5J6W

NMR structures of hylin-a1 analogs: Hylin-K

Summary for 5J6W

• Entry DOI: 10.2210/pdb5j6w/pdb
• Related: 5J6T 5J6V
• NMR Information: BMRB: 30060
• Descriptor: Hylin-K (1 entity in total)
• Functional Keywords: hylin-a1 analogues, antimicrobial peptides, dpc, antimicrobial protein
• Biological source: Hypsiboas albopunctatus (Spotted tree frog)
• Total number of polymer chains: 1
• Total formula weight: 2067.61

Authors

Crusca Jr., E.,Matos, C.O.,Liao, L.M.,Oliveira, A.L. (deposition date: 2016-04-05, release date: 2017-04-12, Last modification date: 2024-10-23)

Primary citation

Crusca, E.,Camara, A.S.,Matos, C.O.,Marchetto, R.,Cilli, E.M.,Liao, L.M.,Lima de Oliveira, A.
NMR structures and molecular dynamics simulation of hylin-a1 peptide analogs interacting with micelles.
J. Pept. Sci., 23:421-430, 2017

PubMed Abstract: 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 -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.

PubMed: 28425152
DOI: 10.1002/psc.3002

Experimental method

SOLUTION NMR