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NMR structures and molecular dynamics simulation of hylin‐a1 peptide analogs interacting with micelles
Author(s) -
Crusca Edson,
Câmara Amanda Souza,
Matos Carolina Oliveira,
Marchetto Reinaldo,
Cilli Eduardo Maffud,
Lião Luciano Morais,
Lima de Oliveira Aline
Publication year - 2017
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.3002
Subject(s) - micelle , peptide , molecular dynamics , chemistry , antimicrobial peptides , biophysics , membrane , nuclear magnetic resonance spectroscopy , helix (gastropod) , combinatorial chemistry , stereochemistry , biochemistry , organic chemistry , computational chemistry , biology , ecology , aqueous solution , snail
Antimicrobial peptides are recognized candidates with pharmaceutical potential against epidemic emerging multi‐drug resistant bacteria. In this study, we use nuclear magnetic resonance spectroscopy and molecular dynamics simulations to determine the unknown structure and evaluate the interaction with dodecylphosphatidylcholine (DPC) and sodium dodecylsulphate (SDS) micelles with three W 6 ‐Hylin‐a1 analogs antimicrobial peptides (HyAc, HyK, and HyD). The HyAc, HyK, and HyD bound to DPC micelles are all formed by a unique α ‐helix structure. Moreover, all peptides reach the DPC micelles' core, which thus suggests that the N‐terminal modifications do not influence the interaction with zwiterionic surfaces. On the other hand, only HyAc and HyK peptides are able to penetrate the SDS micelle core while HyD remains always at its surface. The stability of the α ‐helical structure, after peptide‐membrane interaction, can also be important to the second step of peptide insertion into the membrane hydrophobic core during permeabilization. Copyright © 2017 European Peptide Society and John Wiley & Sons, Ltd.