Volume 232, 2021

Spiers Memorial Lecture: Analysis and de novo design of membrane-interactive peptides

Abstract

Membrane–peptide interactions play critical roles in many cellular and organismic functions, including protection from infection, remodeling of membranes, signaling, and ion transport. Peptides interact with membranes in a variety of ways: some associate with membrane surfaces in either intrinsically disordered conformations or well-defined secondary structures. Peptides with sufficient hydrophobicity can also insert vertically as transmembrane monomers, and many associate further into membrane-spanning helical bundles. Indeed, some peptides progress through each of these stages in the process of forming oligomeric bundles. In each case, the structure of the peptide and the membrane represent a delicate balance between peptide–membrane and peptide–peptide interactions. We will review this literature from the perspective of several biologically important systems, including antimicrobial peptides and their mimics, α-synuclein, receptor tyrosine kinases, and ion channels. We also discuss the use of de novo design to construct models to test our understanding of the underlying principles and to provide useful leads for pharmaceutical intervention of diseases.

Graphical abstract: Spiers Memorial Lecture: Analysis and de novo design of membrane-interactive peptides

Associated articles

Article information

Article type
Paper
Submitted
01 Sep 2021
Accepted
03 Sep 2021
First published
25 Oct 2021

Faraday Discuss., 2021,232, 9-48

Spiers Memorial Lecture: Analysis and de novo design of membrane-interactive peptides

H. T. Kratochvil, Robert W. Newberry, B. Mensa, M. Mravic and W. F. DeGrado, Faraday Discuss., 2021, 232, 9 DOI: 10.1039/D1FD00061F

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