NMR structures and molecular dynamics simulation of hylin-a1 peptide analogs interacting with micelles

Crusca Junior, Edson; Câmara, Amanda Souza; Matos, Carolina Oliveira; Marchetto, Reinaldo; Cilli, Eduardo Maffud; Liao, Luciano Morais; Oliveira, Aline Lima de

NMR structures and molecular dynamics simulation of hylin-a1 peptide analogs interacting with micelles

Data

2017

Autores

Crusca Junior, Edson

Câmara, Amanda Souza

Matos, Carolina Oliveira

Marchetto, Reinaldo

Cilli, Eduardo Maffud

Liao, Luciano Morais

Oliveira, Aline Lima de

Resumo

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 W6-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.

Palavras-chave

W6-Hylin-a1 analogs, NMR, Antimicrobial peptides, Molecular dynamics simulations, DPC, SDS

Citação

CRUSCA JUNIOR, Edson et al. NMR structures and molecular dynamics simulation of hylin-a1 peptide analogs interacting with micelles. Journal of Peptide Science, Hoboken, v. 23, n. 6, p. 421-430, 2017. DOI: 10.1002/psc.3002. Disponível em: https://onlinelibrary.wiley.com/doi/10.1002/psc.3002. Acesso em: 29 jan. 2024.