Rapid Formation of Peptide/Lipid Coaggregates by the Amyloidogenic Seminal Peptide PAP_248-286.

ABSTRACT: Protein/lipid coassembly is an understudied phenomenon that is important to the function of antimicrobial peptides as well as the pathological effects of amyloid. Here, we study the coassembly process of PAP_248-286, a seminal peptide that displays both amyloid-forming and antimicrobial activity. PAP_248-286 is a peptide fragment of prostatic acid phosphatase and has been reported to form amyloid fibrils, known as semen-derived enhancer of viral infection (SEVI), that enhance the viral infectivity of human immunodeficiency virus. We find that in addition to forming amyloid, PAP_248-286 much more readily assembles with lipid vesicles into peptide/lipid coaggregates that resemble amyloid fibrils in some important ways but are a distinct species. The formation of

SUBMITTER: Vane EW 

PROVIDER: S-EPMC7474197 | biostudies-literature | 2020 Sep

REPOSITORIES: biostudies-literature