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    New biotech company giving private-sector boost to SA drug development research

    New biotech company giving private-sector boost to SA drug development research

    SolubleBioScience has yet to move its headquarters to San Antonio, but it’s already having a direct impact on advancing drug development in the Alamo City. The Birmingham, Alabama-based biotech company, recently acquired by CytoBioscience, is contributing new technology to the Center for Innovative Drug Discovery that could prove to be a game changer for researchers and patients.

    SolubleBioScience, a new wholly owned subsidiary of CytoBioscience, has developed an instrument called the HSC, which uses proprietary technology to combine high throughput analytical capabilities with a predictive algorithm to optimize protein formulations.

    The gesture by CytoBioscience and SolubleBioScience is part of a larger effort by the two companies to bring more private-sector support to the Center for Innovative Drug Discovery – or CIDD – and to San Antonio’s bioscience sector.

    UT Health President Dr. William Henrich said the HSC instrument, the first of its kind in the world, will expedite San Antonio scientists’ efforts to move research findings from the laboratory to discovery and ultimately to patient treatments. The instrument, which costs $225,000 each, represents a significant advancement in science, shortening the formulation process from a full year to less than two months.

    James Garvin – CEO of CytoBioscience, which moved its headquarters from Germany to San Antonio in 2015 – said the HSC will improve the accuracy and expediency of research work at the CIDD.

    I previously reported that CytoBioscience plans to move SolubleBioScience from Birmingham to San Antonio before the end of the year. That’s a key reason why UT Health and UTSA are the first academic institutions in the world to get SolubleBioScience’s HSC technology.

    “One of the things I believe with all my heart is that we have to be good corporate citizens and we have to work with our community partners,” Garvin said. “UT Health is one of our best partners. So, to me, this was a no brainer. This is great technology. We wanted to work with one of our partners who could really use it and see what we can do together.”

    Bruce Nicholson, founder of the CIDD, said the gift will go to the center’s High Throughput/Content Screening facility on UT Health’s campus.

    “It’s the second gift we have received from CytoBioscience,” Nicholson said. “What this new instrument will do is allow high throughput testing of solubilities. Many drugs need to be in high concentrations to be effective, but you can only get them to limited concentrations in a lab setting.”

    Nicholson is particularly impressed with the fact that help is coming from a pair of companies still getting their bearings in San Antonio.

    “It’s truly unprecedented,” he said “Normally, academic institutions are not going to get access to this [technology]. But I think CytoBioscience’s whole concept is that the best way to advance drug discovery is to build instruments that have industrial applications but to also share them with academia, which can fuel the enterprise and continue to generate discoveries. So this is very generous of them. But it’s also forward thinking.”

    Matt Hart, director of the CIDD’s high throughput screening facility, said the HSC will add a new dimension to the center’s capabilities.

    “This further emphasizes the importance of academic and industry collaboration,” he said. “This type of collaboration is going to be key in growing the bioscience industry in San Antonio.”

    2 Predictors of Formulation Success Examined

    2 Predictors of Formulation Success Examined


    Protein-Protein Interaction Measurement: Balancing Complete Characterization with High-Throughput Capability in Formulation Development:



    High throughput screening in the world of pharmaceutical development has dramatically increased the number of approved drugs in the last 20 years, and drug developers increasingly use high throughput screening methods as a basis for lead evaluation. This is true in the area of formulation development for biologics, as well, and there are two metrics, Kd and B, that are competing for acceptance as the best predictor of formulation success in terms of stability, aggregation, and viscosity.

    This paper will look at some recent literature focused on measuring Kd (Diffusion Interaction Coefficient) in a high throughput manner to predict formulation success. The acknowledged problems revealed in the discussion of each papers’ results yield valuable insights into the complexity involved in characterizing protein-protein interactions.

    It is well established that a dilute solution thermodynamic parameter, the osmotic second virial coefficient (B value), has quantitative and predictive properties regarding both protein crystallization and protein solubility behavior. For example, to increase the probability of successful crystallization of protein, the crystallization solution should have a B value in the range of approximately -8.0 to -0.2 mol mL/g2 which is referred to as the “crystallization slot” in the literature (Acta Crystallogr D Biol Crystallogr. 1994 Jul 1;50(Pt 4):361-5). As the B value of the crystallizing solution becomes more negative, protein-protein interactions become stronger, often to the point that a shower of crystals, or even amorphous precipitates, form.

    For more positive B values, protein-protein repulsion increases so that the formation of crystal nuclei, or amorphous aggregates, is more difficult (i.e. the solubility of the protein increases). It is exactly this condition – more positive B values – that is beneficial in protein formulations where solubility and stability are of paramount importance.

    It is important to realize that B behavior mimics solubility behavior but does not predict absolute solubility. For example, if it is desired to know how pH affects the solubility of a certain protein, then measuring B value as a function of pH will give results which mimic the solubility behavior as a function of pH. This will be true for any solution variable such as temperature or solution additives (excipients). Thus, in general, solution conditions which increase the B value will result in an increase in protein solubility, or vice versa.

    Since B value is established as a good predictor of protein solubility behavior, the question arises whether or not an experimental platform can be derived to accurately measure B value in a high throughput (HT) manner appropriate for formulation screening. Although HT is a vaguely defined term in formulation development, it is generally thought to mean minimum protein consumption, minimum time consumption, and minimally hands-on instrument operation per B value measurement.

    Traditional methods for B value measurement include membrane osmometry, analytical ultracentrifugation (AUC), and static light scattering (SLS), and the majority of the work proving B value related to protein crystallization and protein solubility behavior has been performed using SLS. However, none of the above-listed methods meet the general expectations of HT. Recently, two approaches are touted as being capable for use as a screening tool for protein formulations – dynamic light scattering (DLS) and self-interaction chromatography (SIC).

    DLS measures scattered intensity fluctuations in a protein solution (as opposed to absolute scattered intensities required in SLS). Since non-absolute measurements are generally easier to determine than absolute measurements, DLS is inherently easier to perform and less fraught with the experimental rigors required of SLS. The experimental protocol for using DLS as a screening tool for protein formulation is to measure the apparent translational diffusion coefficient, Dapp, as a function of protein concentration in a defined solution condition. The data is then cast as:

    Dapp = D°(1 + kDc)
    D° = infinite dilute value for the translational diffusion coefficient
    c = protein concentration (mg/mL)
    kD = diffusion / interaction virial coefficient (mL/g)

    The value of kD is determined from the slope of a plot of Dapp vs. concentration, where D° is the extrapolated intercept and the slope is D°kD. The interaction coefficient, kD, is comprised of two contributions – a thermodynamic contribution via B value, and a hydrodynamic contribution via the frictional factor, kf, for the protein. The frictional factor is dependent on protein size and shape, and does itself have concentration dependence. In certain solution conditions, if the thermodynamic contribution to kD dominates, then clearly the kD value will closely reflect the B value and trends in kD will mimic trends in B value.

    However, for most solution conditions, there is no apriori way of knowing the relative contributions to kD of the thermodynamic and hydrodynamic terms. Thus, to extract B value from a kD measurement becomes ambiguous unless the hydrodynamic contribution is known.

    Measurement of B values, the sum of all interactive forces at all distances and orientations, can be written in terms of the diffusion coefficient (Kd), the friction coefficient (Kr) and volume (V):
    B = (Kd + Kr + v)/2M
    It is apparent in this form of the equation that Kd only represents a portion of the interactive forces in a protein formulation.

    Recent Literature

    Summarized below are some of the pertinent findings from recent publications.

    1. Weak Interactions Govern Viscosity of Concentrated Antibody Solutions.
    Connolly, et al., Biophysical Journal. (2012) 103, 69-78.

     The authors investigated 29 different mAbs and kD values were determined by using 60 uL aliquots of protein solution in a plate reader at 1, 5, 10, 15 and 20 mg/mL, also using the relationship: Dapp = D°(1 + kDc)
     In addition, sedimentation velocity experiments were performed at similar protein concentrations and the sedimentation interaction parameter, ks, was determined from: 1/Sapp = 1/S°(1 + ksc)
     S° = infinite dilution value of the sedimentation coefficient
     The working equation to estimate B value was: B = (kS + kD +v) / 2M
     From the estimated values of B, an empirical relation between kD and B was obtained for the 29 mAbs: KD = 1.33BM – 8.2
     The authors state that this equation is “not universal but limited to molecular types with similar shapes.” This method for determining B, although complete due to the direct measurement of both ks and kd, uses large quantities of protein and is not amenable to high-throughput derivation of B

    2. The Role of Electrostatics in Protein-Protein Interactions of a mAb.
    Roberts, et al., Molecular Pharmaceutics (2014) 11, 2475-2489.

    The authors sought to compare B measurements done by SLS to kD measurements performed using a DLS plate reader. It was noted that “the main motivation for measuring B is that is provides a direct link to protein-protein interaction, whereas the link to kD is less well established, especially for particles with non-spherical shapes.” This is due to the fact that the friction factors are ill defined. In the context of protein-protein interactions of a formulation the kD captures only a partial component of the forces involved. The finding by Roberts et al highlights the incompleteness of kD when identifying protein-protein interactions of a given formulation.

    3. Temperature-Ramped Studies on the Aggregation, Unfolding, and Interaction of a Therapeutic Monoclonal Antibody.Menzen and Friess, JOURNAL OF PHARMACEUTICAL SCIENCES 103:445–455, 2014

     In this 2013 investigation of temperature dependent antibody behavior, Menzen et al develop an empirical relationship between B and kd, similar in purpose to the relationship developed by Connolly, et al. However, the relationships differ with the Menzen paper identifying the following relationship (R2 = 0.85): kd = 1.19BM – 6.29

     In addition to identifying a significantly different relationship between B and kd the authors find the relationship did not hold for the Fab fragment. And state this, “might be a hint that the TIM *transformation of interaction parameters of MAbs] equation is valid only for the full MAbs and cannot be transferred to individual Fab fragments.”

    4. Prediction of Colloidal Stability of High Concentration Protein Formulations.
    Garidel, et al., Pharmaceutical Development and Technology. (2014) e-pub

    The authors measured kD at 1 to 5 mg/mL to predict colloidal stability at 200 mg/mL. Accelerated colloidal stress was imposed by stirring at 5000rpm for 1-3 hours, but results were not conclusive. In contrast to the Connolly paper mentioned above, this paper evaluates kd as a substitute rather than component (with ks) of B. Kd as a substitute for B value is only appropriate under the limited circumstance where sedimentation interaction does not significantly contribute to B value. It was noted that “whereas it is possible to differentiate between net attractive and net repulsive forces by the sign for B, this is not possible for kD.” Results showed that opalescence was as good a predictor as kD and opalescence measurements were used to rank the high concentration solutions (220 mg/mL).

    5. Viscosity of High Concentrations of Monoclonal Antibodies
    Neergaard, et al., European Journal of Pharmaceutical Sciences 49 (2013) 400–410.

    The authors used DLS via a plate reader with 35 uL per well at concentrations of 12 mg/mL and below to estimate kD. There was no quantitative comparison between kd and established measurements of protein-protein interactions. This paper concluded with a suggestion that “the measurement of relative radius we presented as a tool to determine PPI at both low and high concentration may serve as a useful screening tool in high concentration formulation development.” While apparent hydrodynamic radius (rh), and kd are relatively easy to measure it would take exceptionally strong quantitative evidence to substitute a thermodynamic parameters for a simple secondary measurement such as rh.

    Shi, et al., Int. J. Biol. Macromol. (2013) 62, 487-93.

    In this paper, kD was investigated as a B value surrogate for mAbs. The working relation used was
    KD = 2MB-kf-v
    M = molecular weight of protein (g/mol)
    V = partial specific volume of the protein (mL/g)
    KD, B, and kf previously defined

     The authors used a 96 well plate reader to measure kD using 100uL/sample and protein concentrations up to 25mg/mL.
     When performing DLS measurements in quadruplicate in a 96-well plate reader format, Shi notes that “the compounded (D & cp) variability of Kd measurements (by a DLS plate reader) may compromise its ability in determining close protein-protein interactions….” Compared to B measurements made via SIC, there is a single
    experimentally derived factor, the chromatographic retention factor K’, which results in less ambiguity. In Shi’s study, it was determined that “plate based (Kd) measurement failed to unambiguously determine equivalence or difference from 3 different batches of mAbs expected to have very similar Kd values,…”

    Additionally Shi, et al suggests, “To differentiate close interactions, alternative approaches may be pursued such as cuvette-based KD measurement which could effectively reduce location variability from the diffusion coefficient measurement since a single cuvette would be used for all concentrations. Other orthogonal or complementary methods may also be considered…” While cuvettes can provide increased accuracy, the approach would negate the high-throughput nature of the plate based measurements. Orthogonal methods, such as sedimentation velocity studies, can give a complete thermodynamic and hydrodynamic assessment of B value, but at the cost of additional protein and time.


    The diffusion coefficient, Kd, provides a partial indication of protein-protein interaction. Unfortunately, it does not account for the complete set of forces involved in protein-protein interactions. In limited situations where protein-protein interactions are dominated by diffusion components, Kd could serve as a useful proxy for B. Connolly notes, “the empirical relationship between kD and B2 is not universal but limited to molecular types with similar shapes (e.g., IgGs).

    Determination of B2 across molecular types will necessitate an independent determination of both kD and kS…” On the other hand, direct measurements of B, such as SIC and SLS, account for the sum of all forces in protein-protein interactions. While Kd can be supplemented by additional AUC information to determine B value, the additional methods required for complete measurement of protein-protein interactions negatively impacts the high-throughput nature of the method. With the introduction of high-throughput methods for the determination of B value, such as the HSC Technology, it is now possible to accurately measure all of the variables that contribute to protein-protein interactions using a low concentration and volume of protein with a single measurement in a short period of time.

    Southern Biologics Network Established to Create Biologics Faster and Less Expensively

    Southern Biologics Network Established to Create Biologics Faster and Less Expensively

    by Danielle Ragas, ProteoVac PR

    Birmingham, Baton Rouge, Raleigh and Research Triangle Park — Five biopharmaceutical research organizations with operations in Birmingham, Baton Rouge, Raleigh and Research Triangle Park have formed a new public-private partnership called the Southern Biologics Network (SBN) to create biologics faster and less expensively.

    The five research organizations will work together to create advanced biologics for biopharmaceutical companies of all sizes.

    Biologics are genetically engineered proteins from plant, animal and human cells. They’ll be used to create therapeutics, vaccines, diagnostics and drug targets to treat and prevent diseases, assist in drug discovery, and improve the lives of tens of thousands of patients across the United States.


    The five research organizations are:

    • Birmingham-based Southern Research Institute, which has created seven FDA-approved cancer drugs. Scientists there are discovering and developing treatments in multiple disease areas including oncology, Parkinson’s, Alzheimer’s, diabetes and infectious diseases.
    • Pennington Biomedical Research Center at Louisiana State University in Baton Rouge is at the forefront of medical discovery on understanding and combating obesity, diabetes, cardiovascular disease, cancer, dementia, and other chronic diseases with the goal of improving human health across the lifespan.
    • The Center for Structural Biology at the University of Alabama at Birmingham is a leading structural biology research center providing scientists with biophysical and structural information on protein and protein/drug complexes.
    • ProteoVec, Inc., in Baton Rouge, Raleigh and RTP. PV’s scientists develop and scale biologics production processes earlier in development, and more cost effectively, than previously possible.
    • Soluble Therapeutics Inc., in Birmingham can determine optimized formulations that maximize solubility and stability for protein-based therapeutics in less than 60 days.

    Biologics have revolutionized the treatment of rheumatoid arthritis, Crohn’s disease, multiple sclerosis and different types of cancers. Development of new biosimilar versions of existing breakthrough biologics are key to making healthcare more affordable and improving outcomes.

    Pharmaceutical Companies Will Bring More Life-Saving Treatments to Market by Using SBN’s Services

    SBN is the first organization in the Southeastern United States to provide truly comprehensive biologic development services. Pharmaceutical companies will be able to save time and money because they’ll be able to select one organization, SBN, instead of trying to coordinate the work of several biopharmaceutical research firms for the manufacture, discovery, preclinical development, and early-stage clinical development of biologics.

    “More affordable production and more mature early-stage process development will lead to a greater number of breakthroughs making it to market,” said ProteoVec CEO Michael Crapanzano, M.D. “Not only does that save time; that saves money, too.”

    That’s a significant point of difference, considering the business risks and costs of drug development. According to the Pharmaceutical Research and Manufacturers of America, it can take up to15 years to create an FDA-approved drug. Research and development costs can exceed $1 billion, and only 20 percent of marketed drugs break even or turn a profit. Still, medicine can make a huge difference. Since 1980, 83 percent of life expectancy gains for cancer patients can be attributed to new treatments. The HIV/AIDS death rate has dropped more than 80 percent since the use of antiretroviral treatments in 1995.

    “SBN combines some of the brightest minds in biologics, helps reduce the risk that pharmaceutical companies take at the earliest stages of biologics discovery and development, and allows our five entities to work together more efficiently with clients to do what we all do best — create biological therapeutics for our customers that will dramatically improve patients’ lives,” said Art Tipton, Ph.D., president and CEO of Southern Research Institute.

    “We are excited to be part of this network, since we have many of the components necessary to quickly advance high value drug targets using our expertise in protein characterization, target validation, and the ability to optimize preclinical candidates for clients,” explained Dr. Larry DeLucas, director of the Center for Structural Biology at UAB.

    About the Southern Biologics Network

    Southern Biologics Network service offerings include: initial characterization of protein structures and protein-drug interactions; protein expression, purification and formulation; preclinical in-vitro/in-vivo IND enabling studies; and Phase I clinical studies. SBN’s customer service focus includes close consulting and assistance in the design and execution of all aspects of early-stage biologic development using cost effective, creative, and customized approaches. For more information, please visit

    Protein solubility can be enhanced at various points along the production pipeline

    Protein solubility can be enhanced at various points along the production pipeline

    by Michelle Amaral, Science Writer

    This article, written by our Science Writer/PR Consultant, was published in the September 2013 issue of ON drugDelivery Magazine. We are excited that this issue will be circulated at the 3rd Annual PODD – Partnership Opportunities in Drug Delivery – Conference in Boston and at the CPhI Worldwide Pharma Expo CPhI Worldwide Pharma Expo

    In this piece, we summarize some of the techniques available for the generation of different formulations of recombinant protein therapeutics, and high-throughput technologies that reduce the time required to screen for the optimal formulation.

    A revolutionary moment for the pharmaceutical industry occurred with the advent of recombinant technologies, which enabled proteins to be manufactured and then delivered to humans or animals for the purpose of treating illness and disease. As a result, a wide range of therapeutic approaches opened up: aberrant proteins causing a disease state could be replaced; novel proteins combatting a particular disease could be introduced; and delivery of small-molecule pharmaceuticals could be enhanced through conjugation to a protein or antibody.

    In the late 1970s, insulin was the first human protein to be produced using genetic engineering technologies and became commercially available in 1982, greatly advancing the treatment of diabetes. However, the use of proteins in therapeutic strategies presents a number of challenges, namely the requirement that a protein be highly concentrated, stable, and active in solution when delivered.

    Fresh, innovative approaches are now providing valuable solutions for protein pharmaceuticals. The aforementioned challenges can be confronted at various points along the path of protein production. In the early stages of development, a protein’s solubility can be affected by the choice of expression vector and the option of adding a fusion tag to the protein of interest. Further downstream, self-interaction chromatography (SIC) is being used as a fast and effective method for determining the most optimal formulation of a protein solution.

    The selection of a high-performance expression vector is a must when creating a strategy for recombinant protein production, as it can play an integral role in promoting a soluble product in addition to an optimal yield. In many cases, these vectors encode for extra amino acids that are then attached, or fused, to the prtotein of interest upon expression. The result is a fusion protein with greater solubility than that of the native macromolecule expressed alone. Oftentimes, the fusion partner even contains a region of histidine “tags” that enable quick, efficient purification with affinity chromatography and a cleavage site that allows its subsequent removal using a specific protease treatment.

    A fusion partner can range in size from a few amino acids to approximately 25 kDa. The added residues create disorder, allowing greater distance between each protein molecule and thus giving the protein of interest “space” to fold properly. This process enhances solubility of the target protein and prevents aggregation. Activity assays have been performed on numerous representative proteins, demonstrating that functionality is preserved.

    Protein solubility can also be enhanced after its production by formulating a buffer solution with conditions that are optimal for proper folding and stability. This is an important step along the light scattering effects of some additives. SIC requires a small amount of protein that is covalently attached to beads and packed into a microcapillary HPLC column. The mobile phase of the SIC experiments consists of the formulation being tested, along with a 1uL bolus injection of the protein of interest. The elution of the protein injected in the mobile phase is measured via UV detection and the retention time is used to evaluate whether or not the formulation or additive of interest is causing attraction or repulsion between the protein molecules.

    Data collected via SIC enables the calculation of a parameter that quantitatively describes the protein’s interaction with itself; this is the second virial coefficient, or B value. The B value is the sum of all potential forces between two proteins including ionic, dipole, hydrophobic, and van der Waals forces; it is a measure of protein flexibility in all orientations and distances. In general, positive B values indicate a net repulsion between two protein molecules while negative B values indicate a net attraction. When additives are introduced into solutions, the B value is altered such that the protein molecules display mild attraction to each other, which is conducive to crystallization, or enhanced repulsion, which increases the protein’s physical stability and solubility.

    Experimentally determined B values can be used to predict the B value of a protein in over 12,000 other formulations using an artificial neural network. This is a wealth of information for groups that are developing a new biopharmaceutical. Differential scanning calorimetry and other biophysical techniques are performed to confirm a complete characterization profile on the final solutions.

    Treatments for disease have drastically improved since the advent of protein therapeutics. In order to be successful, though, a protein must be highly concentrated, stable, and active in solution without aggregation or other phase changes that are detrimental to the drug delivery process and the patient. Solubility can be enhanced at several points along the protein production pipeline. Creating disorder by fusing extra amino acid residues to the protein of interest generates distance between each molecule, enhancing the ability of the protein to fold correctly. An optimal formulation for the protein of interest is crucial for protein performance as well.

    High-throughput methods that screen components of the solution save time and money for a company developing a promising drug.

    Tackling the Problems of Insolubility

    Tackling the Problems of Insolubility

    by Carol Potera

    Companies developing Biosciences face the challenge of how to keep therapeutic proteins soluble, stable, and active. About half of all recombinant proteins are insoluble, a major hurdle for advancing them through drug discovery pipelines and into clinical trials. Unlike small molecule drugs, proteins also easily degrade. Whereas insolubility reduces the dose and effectiveness of biotherapeutics, degradation byproducts can cause serious side effects.

    Soluble Therapeutics Inc. uses its HSC™ technology (somewhat short for high-throughput second virial coefficient determination) to optimize protein formulations and speed their development. “Our solution reduces the time and manpower required to make proteins highly soluble and physically stable,” says Joseph Garner, Ph.D., CEO.

    Conventional methods to formulate soluble and stable proteins often cost hundreds of thousands of dollars and require, on average, a team of five people working a year or longer, Dr. Garner notes. “Our technology takes 45 days, and we charge $30,000 to $35,000 per protein. It’s an incredibly efficient way to get past the roadblock of solubility,” he says. Moreover, HSC requires about 25 milligrams of a protein for formulation, compared to a gram or more for standard methods.

    HSC technology uses thermal dynamics principles to predict the solubility of proteins under a variety of solution conditions. Robots, liquid-handling equipment, and an artificial neural network perform in silico modeling of 12,000 solution conditions. The goal is to identify optimal combinations of additives and excipients that increase solubility, physical stability, and protein concentrations. Dr. Garner says that Soluble Therapeutics Inc. helped one client to increase the concentration of a lead monoclonal antibody candidate 150-fold, and it’s now in clinical trials.

    Soluble recently received an award of about $1 million from the NIH Small Business Technology Transfer Program, which the firm says will allow it to accelerate the further development and commercialization of HSC technology.

    Larry DeLucas, Ph.D., director of the Center for Biophysical Sciences and Engineering at the University of Alabama at Birmingham, and Bill Wilson, Ph.D., at Mississippi State University, invented HSC and co-founded Soluble Therapeutics in 2008. They initially used the HSC technology to crystallize proteins (a highly insoluble state) to determine their 3D structures. Later they reversed the technology to make proteins highly soluble. Soluble Therapeutics can help to determine 3D structures of proteins for clients, too.

    The company currently operates as a CRO, but plans to sell its third-generation HSC instrument. “We will always perform contract formulation services,” says Dr. Garner, “but some companies want to do this process themselves.” Customers will buy the benchtop HSC instrument and disposables, then connect to Soluble Therapeutics’ shared artificial neural network to perform calculations and receive results within a day. The firm expects to release the benchtop HSC system this fall.

    To read the Genetic Engineering & Biotechnology News article about The HSCTM Technology, click here

    Soluble Therapeutics, Inc. Awarded ~$1MM NIH Grant for Continued Development of the HSC™  Technology for Protein Formulation

    Soluble Therapeutics, Inc. Awarded ~$1MM NIH Grant for Continued Development of the HSC™ Technology for Protein Formulation


    Birmingham, AL – 1 June 2012 – Soluble Therapeutics, Inc. a Birmingham, Alabama–based CRO specializing in formulation optimization for protein-based Bioscience announces a Phase II award of approximately $1MM from the NIH Small Business Technology Transfer Program (STTR).

    After closing a $1MM round of venture funding in the summer of 2011, this new infusion of capital will allow Soluble Therapeutics to accelerate the development and commercialization of the HSCTM
    Technology for protein formulation – a technology that is able to identify optimized formulations for protein-based Bioscience in 45 days while using minimal quantities of protein. This technology has the power to greatly reduce the time and resources required to prepare protein-based drugs for clinical development.

    Dr. Larry DeLucas, Director of the UAB Center for Biophysical Sciences and Engineering is the principal investigator on the project and is one of the founding scientists of Soluble Therapeutics. Dr. Delucas states that he is “extremely pleased with the direction the company has taken with this technology and this Phase II award is proof of its commercial viability and immediate success in a challenging formulation market.”

    “This grant is another testament to the excellent work in biotechnology that is coming out of Soluble Therapeutics, UAB and being fostered at Innovation Depot,” said Steven Ceulemans, Vice President of Innovation and Technology at the Birmingham Business Alliance, the Birmingham region’s leading economic development agency. “It demonstrates the value of the HSCTM Technology and the strength of the Birmingham region’s innovation infrastructure.”

    Soluble Therapeutics’ CEO, Dr. Joseph Garner states that “our formulation service, utilizing the HSCTM
    Technology, continues to perform well in commercial engagements and this funding from the NIH further validates our technology as a new standard in protein formulation. We look forward to completing the development of the 3
    generation of the HSCTM Instrument that will be made available for purchase to the biopharmaceutical industry.”

    About Soluble Therapeutics, Inc.

    Soluble Therapeutics, Inc. was founded in 2008 to commercialize the HSC™ Technology. The company’s services enhance the drug development process by rapidly optimizing protein solubility and stability, bringing transformational technology to the world of protein-based pharmaceuticals, vaccines, and therapeutics. Led by CEO Dr. Joseph N. Garner, Soluble Therapeutics’ management team consists of science industry professionals bringing over 60 years combined experience from organizations such as NASA, the University of Alabama at Birmingham, and Mississippi State University. Soluble Therapeuticse, Inc. is the first to introduce protein formulation solutions that deliver the price and performance advantages of the HSCTM Technology. For additional information visit

    To read the BioSpace article about The HSCTM Technology, click here