← Back to KHAO

NIST · Open Source ·

Flexible Protein Simulations of Monoclonal Antibodies to Enable Biotherapeutic Development

2 min read

Compiled by KHAO Editorial — aggregated from 1 source. See llms.txt for citation guidance.

★ Tier-1 Source

Dynamic motions of the NISTmAb antibody.

All-atom modeling and dynamics refines design of protein therapeutics by incorporating dynamics in low and high concentration formulations.

Key facts

Summary

In several projects, computational work integrates with experimental work to tell them something about the critical quality attributes of this highly flexible molecule. Grow from the “static sphere” model to interpret experiments. Formulating them at high concentrations is difficult because they tend to cluster and aggregate, which raises viscosity and shortens shelf‑life. Because the hinge is highly flexible and largely unstructured, conventional structural experiments (cryo‑EM, X‑ray crystallography) provide little insight. Additionally, they have determined a method for free energy readout in the Fc domain, a target for modulating effector functions in vivo. Kleczynski, M., Bergonzo, C.*, Kearsley, A.J. Spatial and sequential topological analysis of molecular dynamics simulations of IgG1 Fc domains. Szalai, V., Bergonzo, C.*, Lyon, R., Kelman, Z., Schmidt, T., Grishaev, A.

Read full article at NIST AI →

#NIST #Open Source