ArticleComputational and structural biotechnology journal2021
Comparison of the pH- and thermally-induced fluctuations of a therapeutic antibody Fab fragment by molecular dynamics simulation.
Article in Computational and structural biotechnology journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- Hotspot Interactions between Two Fab Molecules in Molecular Dynamics Simulations Improve Predictive Models of Aggregation Kinetics.Molecular pharmaceutics · 2026Article
- Article
- Stability Testing Reveals Photoselective Clipping of Heavy Chain C-Terminal Amino Acids That Leads to Fragmentation and Aggregation of an Antibody Fab Fragment.Molecular pharmaceutics · 2025Article
- Hinge Truncation to Improve Aggregation Kinetics and Thermal Stability of an Antibody Fab Fragment.Molecular pharmaceutics · 2025Article
- Improved Enzymatic Properties of Chitosanase CsnMY002 fromInternational journal of molecular sciences · 2025Article
- Molecular Dynamics Simulations Reveal How Competing Protein-Surface Interactions for Glycine, Citrate, and Water Modulate Stability in Antibody Fragment Formulations.Molecular pharmaceutics · 2024Article
- Predictive Model Building for Aggregation Kinetics Based on Molecular Dynamics Simulations of an Antibody Fragment.Molecular pharmaceutics · 2024Article
- Crystal structures and molecular dynamics simulations of a humanised antibody fragment at acidic to basic pH.Scientific reports · 2023Article
- Getting Smaller by Denaturation: Acid-Induced Compaction of Antibodies.The journal of physical chemistry letters · 2023Article
- Binding modes of prothrombin cleavage site sequences to the factor Xa catalytic triad: Insights from atomistic simulations.Computational and structural biotechnology journal · 2022Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Successful development of protein therapeutics depends critically on achieving stability under a range of conditions. A deeper understanding of the drivers of instability across different stress conditions, will enable the engineering of more robust protein scaffolds. We compared the impacts of low pH and high temperature stresses on the structure of a humanized antibody fragment (Fab) A33, using atomistic molecular dynamics simulations, using a recent 2.5 Å crystal structure. This revealed that low-pH induced the loss of native contacts in the domain C
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