Thermal stability of single-domain antibodies estimated by molecular dynamics simulations.

ABSTRACT: Single-domain antibodies (sdAbs) function like regular antibodies, however, consist of only one domain. Because of their low molecular weight, sdAbs have advantages with respect to production and delivery to their targets and for applications such as antibody drugs and biosensors. Thus, sdAbs with high thermal stability are required. In this work, we chose seven sdAbs, which have a wide range of melting temperature (T_m ) values and known structures. We applied molecular dynamics (MD) simulations to estimate their relative stability and compared them with the experimental data. High-temperature MD simulations at 400 K and 500 K were executed with simulations at 300 K as a control. The fraction of native atomic contacts, Q, measured for the 400 K simulations showed a fairly good c

SUBMITTER: Bekker GJ 

PROVIDER: S-EPMC6319760 | biostudies-literature | 2019 Feb

REPOSITORIES: biostudies-literature