Experimental evaluation of single-domain antibodies predicted by molecular dynamics simulations to have elevated thermal stability.

ABSTRACT: Recently Bekker et al. [Bekker G-J et al. Protein Sci. 2019;28:429-438.] described a computational strategy of applying molecular-dynamics simulations to estimate the relative stabilities of single-domain antibodies, and utilized their method to design changes with the aim of increasing the stability of a single-domain antibody with a known crystal structure. The structure from which they generated potentially stabilizing mutations is an anti-cholera toxin single domain antibody selected from a naïve library which has relatively low thermal stability, reflected by a melting point of 48°C. Their work was purely theoretical, so to examine their predictions, we prepared the parental and predicted stabilizing mutant single domain antibodies and examined their thermal stability, ability to refo

SUBMITTER: Zabetakis D 

PROVIDER: S-EPMC6739806 | biostudies-literature | 2019 Oct

REPOSITORIES: biostudies-literature