Please use this identifier to cite or link to this item:
Title: Structural Analysis and Design of Chionodracine-Derived Peptides Using Circular Dichroism and Molecular Dynamics Simulations
Authors: Borocci, Stefano 
Della Pelle, Giulia
Ceccacci, Francesca
Olivieri, Cristina
Buonocore, Francesco 
Porcelli, Fernando 
Issue Date: 2020
Antimicrobial peptides have been identified as one of the alternatives to the extensive use of common antibiotics as they show a broad spectrum of activity against human pathogens. Among these is Chionodracine (Cnd), a host-defense peptide isolated from the Antarctic icefish Chionodracohamatus, which belongs to the family of Piscidins. Previously, we demonstrated that Cnd and its analogs display high antimicrobial activity against ESKAPE pathogens (Enterococcus faecium, Staphylococcus aureus, Klebsiella pneumoniae, Acinetobacterbaumannii, Pseudomonas aeruginosa and Enterobacter species). Herein, we investigate the interactions with lipid membranes of Cnd and two analogs, Cnd-m3 and Cnd-m3a, showing enhanced potency. Using a combination of Circular Dichroism, fluorescence spectroscopy, and all-atom Molecular Dynamics (MD) simulations, we determined the structural basis for the different activity among these peptides. We show that all peptides are predominantly unstructured in water and fold, preferentially as α-helices, in the presence of lipid vesicles of various compositions. Through a series of MD simulations of 400 ns time scale, we show the effect of mutations on the structure and lipid interactions of Cnd and its analogs. By explaining the structural basis for the activity of these analogs, our findings provide structural templates to design minimalistic peptides for therapeutics.
ISSN: 1422-0067
DOI: 10.3390/ijms21041401
Appears in Collections:A1. Articolo in rivista

Files in This Item:
File Description SizeFormat Existing users please
P69_ijms_2020.pdf4.03 MBAdobe PDF    Request a copy
Show full item record

Page view(s)

Last Week
Last month
checked on Nov 29, 2021


checked on Nov 29, 2021

Google ScholarTM



All documents in the "Unitus Open Access" community are published as open access.
All documents in the community "Prodotti della Ricerca" are restricted access unless otherwise indicated for specific documents