Search Results - "Brych, Stephen R"

The identification of free cysteine residues within antibodies and a potential role for free cysteine residues in covalent aggregation because of agitation stress by Huh, Joon H, White, April J, Brych, Stephen R, Franey, Heather, Matsumura, Masazumi

“…Human immunoglobulin G1 (IgG1) and immunoglobulin G2 (IgG2) antibodies contain multiple disulfide bonds, which are an integral part of the structure and…”
Get more information

Characterization of antibody aggregation: role of buried, unpaired cysteines in particle formation by Brych, Stephen R, Gokarn, Yatin R, Hultgen, Heather, Stevenson, Riki J, Rajan, Rahul, Matsumura, Masazumi

“…Proteins are susceptible to degradation upon exposure to a variety of stresses during product manufacturing, transportation and storage. In this study, we…”
Get more information

Effect of Ions on Agitation- and Temperature-Induced Aggregation Reactions of Antibodies by Fesinmeyer, R. Matthew, Hogan, Sabine, Saluja, Atul, Brych, Stephen R, Kras, Eva, Narhi, Linda O, Brems, David N, Gokarn, Yatin R

“…Purpose The impact of ions on protein aggregation remains poorly understood. We explored the role of ionic strength and ion identity on the temperature- and…”
Get full text

Increased aggregation propensity of IgG2 subclass over IgG1: Role of conformational changes and covalent character in isolated aggregates by Franey, Heather, Brych, Stephen R., Kolvenbach, Carl G., Rajan, Rahul S.

“…Aggregation of human therapeutic antibodies represents a significant hurdle to product development. In a test across multiple antibodies, it was observed that…”
Get full text

Contributions of a disulfide bond to the structure, stability, and dimerization of human IgG1 antibody CH3 domain by McAuley, Arnold, Jacob, Jaby, Kolvenbach, Carl G., Westland, Kimberly, Lee, Hyo Jin, Brych, Stephen R., Rehder, Douglas, Kleemann, Gerd R., Brems, David N., Matsumura, Masazumi

“…Recombinant human monoclonal antibodies have become important protein‐based therapeutics for the treatment of various diseases. The antibody structure is…”
Get full text

A High Threshold of Biotherapeutic Aggregate Numbers is Needed to Induce an Immunogenic Response In Vitro, In Vivo, and in the Clinic by Cohen, Joseph R., Brych, Stephen R., Prabhu, Siddharth, Bi, Vivian, Elbaradei, Ahmed, Tokuda, Joshua M., Xiang, Cathie, Hokom, Martha, Cui, Xiaohong, Ly, Claudia, Amos, Nathan, Sun, Jilin, Calamba, Dominador, Herskovitz, Jonathan, Capili, Allyson, Nourbakhsh, Kimya, Merlo, Anthony, Carreon, Julia, Wypych, Jette, Narhi, Linda O., Jawa, Vibha, Joubert, Marisa K.

“…Background and Purpose There is concern that subvisible aggregates in biotherapeutic drug products pose a risk to patient safety. We investigated the threshold…”
Get full text

Accommodation of a highly symmetric core within a symmetric protein superfold by Brych, Stephen R., Kim, Jaewon, Logan, Timothy M., Blaber, Michael

“…An alternative core packing group, involving a set of five positions, has been introduced into human acidic FGF‐1. This alternative group was designed so as to…”
Get full text

Symmetric Primary and Tertiary Structure Mutations within a Symmetric Superfold: A Solution, not a Constraint, to Achieve a Foldable Polypeptide by Brych, Stephen R., Dubey, Vikash K., Bienkiewicz, Ewa, Lee, Jihun, Logan, Timothy M., Blaber, Michael

“…In previous studies designed to increase the primary structure symmetry within the hydrophobic core of human acidic fibroblast growth factor (FGF-1) a…”
Get full text

Identification of a Key Structural Element for Protein Folding Within β-Hairpin Turns by Kim, Jaewon, Brych, Stephen R, Lee, Jihun, Logan, Timothy M, Blaber, Michael

“…Specific residues in a polypeptide may be key contributors to the stability and foldability of the unique native structure. Identification and prediction of…”
Get full text

Structure and stability effects of mutations designed to increase the primary sequence symmetry within the core region of a β‐trefoil by Brych, Stephen R., Blaber, Sachiko I., Logan, Timothy M., Blaber, Michael

“…Human acidic fibroblast growth factor (FGF‐1) is a member of the β‐trefoil hyperfamily and exhibits a characteristic threefold symmetry of the tertiary…”
Get full text

Sequence swapping does not result in conformation swapping for the β4/β5 and β8/β9 β‐hairpin turns in human acidic fibroblast growth factor by Kim, Jaewon, Lee, Jihun, Brych, Stephen R., Logan, Timothy M., Blaber, Michael

“…The β‐turn is the most common type of nonrepetitive structure in globular proteins, comprising ∼25% of all residues; however, a detailed understanding of…”
Get full text

Contributions of a disulfide bond to the structure, stability, and dimerization of human IgG1 antibody C H 3 domain by McAuley, Arnold, Jacob, Jaby, Kolvenbach, Carl G., Westland, Kimberly, Lee, Hyo Jin, Brych, Stephen R., Rehder, Douglas, Kleemann, Gerd R., Brems, David N., Matsumura, Masazumi

“…Abstract Recombinant human monoclonal antibodies have become important protein‐based therapeutics for the treatment of various diseases. The antibody structure…”
Get full text

Contributions of a disulfide bond to the structure, stability, and dimerization of human IgG1 antibody C sub(H)3 domain by McAuley, Arnold, Jacob, Jaby, Kolvenbach, Carl G, Westland, Kimberly, Lee, Hyo Jin, Brych, Stephen R, Rehder, Douglas, Kleemann, Gerd R, Brems, David N, Matsumura, Masazumi

“…Recombinant human monoclonal antibodies have become important protein-based therapeutics for the treatment of various diseases. The antibody structure is…”
Get full text

Sequence swapping does not result in conformation swapping for the beta4/beta5 and beta8/beta9 beta-hairpin turns in human acidic fibroblast growth factor by Kim, Jaewon, Lee, Jihun, Brych, Stephen R, Logan, Timothy M, Blaber, Michael

“…The beta-turn is the most common type of nonrepetitive structure in globular proteins, comprising ~25% of all residues; however, a detailed understanding of…”
Get full text