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stability
ARGEN_PEGS Boston 2018

Formulating Four Peptides: ARGEN Application Note 005

Formulation of Four Peptide Solutions in 15 Days Background Custom designed oligopeptides are an increasingly accessible option in peptide-based technologies for pharmaceuticals. Following their synthesis, peptides are often subjected to HPLC purification and synthetic modification, which can require the use of non-aqueous media or salts requiring later removal. During the production of pharmaceutical peptides, spoilage...
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ARGEN_PEGS Boston 2018

Kinetic Analysis of Peptide Aggregation: ARGEN Application Note 004

Kinetic Analysis of Peptide Aggregation Background Peptide-based pharmaceutical technology requires the delivery of therapeutic oligopeptides as designed in a stable form for effective application. Downstream from therapeutic peptide isolation or synthesis, peptides are often subjected to HPLC purification, synthetic modification, and preparatory treatments for long-term storage. Spoilage in the form of aggregation, degradation or oxidation...
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ARGEN_PEGS Boston 2018

Determining Mw and B22 of mAbs: ARGEN Application Note 003

Determining Molecular Weight (Mw) and Second Virial Coefficient (B22) of monoclonal antibodies using ARGEN Abstract Protein aggregation is generally believed to occur as the result of two instability factors—  conformational and colloidal. Conformational stability is the difference in free energy between the folded and unfolded states of a protein. Although not directly measured as a...
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ARGEN_PEGS Boston 2018

Formulation Development: ARGEN Application Note 002

Formulation Development with ARGEN Abstract Formulations are developed in the biopharmaceutical space as a set of solution conditions that lead to the highest stability of a therapeutic substance such as an antibody protein or peptide.  The solution conditions that generally affect the stability of the solute are solvent choice, ionic strength, pH, excipient, surfactant and...
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FA_Product_ARGEN

Comparing Protein Stability: ARGEN Application Note 001

Comparing the Stability of Protein Formulations with ARGEN Abstract Because ARGEN’s 16 experiments are fully independent, users can determine aggregation or degradation characteristics of protein formulations for all samples simultaneously, regardless of their individual time spans (some can take minutes, others can take weeks). When one sample is complete, another can immediately take its place....
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