Investigating the Disordered and Membrane-Active Peptide A-Cage-C Using Conformational Ensembles.

ABSTRACT: The driving forces and conformational pathways leading to amphitropic protein-membrane binding and in some cases also to protein misfolding and aggregation is the subject of intensive research. In this study, a chimeric polypeptide, A-Cage-C, derived from α-Lactalbumin is investigated with the aim of elucidating conformational changes promoting interaction with bilayers. From previous studies, it is known that A-Cage-C causes membrane leakages associated with the sporadic formation of amorphous aggregates on solid-supported bilayers. Here we express and purify double-labelled A-Cage-C and prepare partially deuterated bicelles as a membrane mimicking system. We investigate A-Cage-C in the presence and absence of these bicelles at non-binding (pH 7.0) and binding (pH 4.5) conditions. Using i

SUBMITTER: Dobrovolska O 

PROVIDER: S-EPMC8231226 | biostudies-literature | 2021 Jun

REPOSITORIES: biostudies-literature