5MXT

Peptide-membrane interaction between targeting and lysis

Summary for 5MXT

• Entry DOI: 10.2210/pdb5mxt/pdb
• NMR Information: BMRB: 34092
• Descriptor: TRP-TYR-HIS-ARG-LEU-SER-HIS-ILE-HIS-SER-ARG-LEU-GLN-ASP-NH2 (1 entity in total)
• Functional Keywords: protein, cell cycle
• Biological source: synthetic construct
• Total number of polymer chains: 1
• Total formula weight: 1851.08

Authors

Schneider, G.,Blatter, M. (deposition date: 2017-01-24, release date: 2017-02-22, Last modification date: 2024-11-20)

Primary citation

Stutz, K.,Muller, A.T.,Hiss, J.A.,Schneider, P.,Blatter, M.,Pfeiffer, B.,Posselt, G.,Kanfer, G.,Kornmann, B.,Wrede, P.,Altmann, K.H.,Wessler, S.,Schneider, G.
Peptide-Membrane Interaction between Targeting and Lysis.
ACS Chem. Biol., 12:2254-2259, 2017

PubMed Abstract: Certain cationic peptides interact with biological membranes. These often-complex interactions can result in peptide targeting to the membrane, or in membrane permeation, rupture, and cell lysis. We investigated the relationship between the structural features of membrane-active peptides and these effects, to better understand these processes. To this end, we employed a computational method for morphing a membranolytic antimicrobial peptide into a nonmembranolytic mitochondrial targeting peptide by "directed simulated evolution." The results obtained demonstrate that superficially subtle sequence modifications can strongly affect the peptides' membranolytic and membrane-targeting abilities. Spectroscopic and computational analyses suggest that N- and C-terminal structural flexibility plays a crucial role in determining the mode of peptide-membrane interaction.

PubMed: 28763193
DOI: 10.1021/acschembio.7b00504

Experimental method

SOLUTION NMR