title: Cationic membrane peptides: atomic-level insight of structure-activity relationships from solid-state NMR.
abstract: Many membrane-active peptides, such as cationic cell-penetrating peptides (CPPs) and antimicrobial peptides (AMPs), conduct their biological functions by interacting with the cell membrane. The interactions of charged residues with lipids and water facilitate membrane insertion, translocation or disruption of these highly hydrophobic species. In this review, we will summarize high-resolution structural and dynamic findings towards the understanding of the structure-activity relationship of lipid membrane-bound CPPs and AMPs, as examples of the current development of solid-state NMR (SSNMR) techniques for studying membrane peptides. We will present the most recent atomic-resolution structure of the guanidinium-phosphate complex, as constrained from experimentally measured site-specific distances. These SSNMR results will be valuable specifically for understanding the intracellular translocation pathway of CPPs and antimicrobial mechanism of AMPs, and more generally broaden our insight into how cationic macromolecules interact with and cross the lipid membrane.
authors.affiliation: Department of Chemistry, Iowa State University, Ames, IA 50011, USA. ycsu@mit.edu
authors.forename: Yongchao
authors.initials: Y
authors.lastname: Su
authors.forename: Shenhui
authors.initials: S
authors.lastname: Li
authors.forename: Mei
authors.initials: M
authors.lastname: Hong
mesh_terms: D000818:Animals; D023181:Antimicrobial Cationic Peptides / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology*; D002462:Cell Membrane / Q000737:chemistry / Q000378:metabolism*; D057846:Cell-Penetrating Peptides / Q000737:chemistry* / Q000378:metabolism / Q000494:pharmacology*; D006801:Humans; D009682:Magnetic Resonance Spectroscopy; D013329:Structure-Activity Relationship
chemical_list: D023181:Antimicrobial Cationic Peptides; D057846:Cell-Penetrating Peptides