Cooperative Induction of Ordered Peptide and Fatty Acid Aggregates.
Ontology highlight
ABSTRACT: Interactions between biological membranes and disease-associated amyloids are well documented, and their prevalence suggests that an inherent affinity exists between these molecular assemblies. Our interest in the molecular origins of life have led us to investigate the nature of such interactions in the context of their molecular predecessors (i.e., vesicle-forming amphiphiles and small peptides). Under certain conditions, amyloidogenic peptides or fatty acids are each able to form ordered structures on their own; however, we report here on their cooperative assembly into novel, to our knowledge, highly ordered structures. We first examined an amyloidogenic eight-residue peptide, which forms amyloids at pH 11, yet because of its positive electrostatic character remains soluble at a neutra
SUBMITTER: Bomba R
PROVIDER: S-EPMC6302236 | biostudies-literature | 2018 Dec
REPOSITORIES: biostudies-literature
ACCESS DATA