Targeting S100B with Peptides Encoding Intrinsic Aggregation-Prone Sequence Segments.

ABSTRACT: S100 proteins assume a diversity of oligomeric states including large order self-assemblies, with an impact on protein structure and function. Previous work has uncovered that S100 proteins, including S100B, are prone to undergo β-aggregation under destabilizing conditions. This propensity is encoded in aggregation-prone regions (APR) mainly located in segments at the homodimer interface, and which are therefore mostly shielded from the solvent and from deleterious interactions, under native conditions. As in other systems, this characteristic may be used to develop peptides with pharmacological potential that selectively induce the aggregation of S100B through homotypic interactions with its APRs, resulting in functional inhibition through a loss of function. Here we report initial studie

SUBMITTER: Cristovao JS 

PROVIDER: S-EPMC7830867 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature