Please use this identifier to cite or link to this item:
Title: Fish-derived antimicrobial peptides: Activity of a chionodracine mutant against bacterial models and human bacterial pathogens
Authors: Buonocore, Francesco 
Picchietti, Simona 
Porcelli, Fernando 
Della Pelle, Giulia
Olivieri, Cristina
Poerio, Elia 
Bugli, Francesca
Menchinelli, Giulia
Sanguinetti, Maurizio
Bresciani, Alberto
Gennari, Nadia
Taddei, Anna Rita
Fausto, Anna Maria 
Scapigliati, Giuseppe 
Issue Date: 2019
The increasing resistance to conventional antibiotics is an urgent problem that can be addressed by the discovery of new antimicrobial drugs such as antimicrobial peptides (AMPs). AMPs are components of innate immune system of eukaryotes and are not prone to the conventional mechanisms that are responsible of drug resistance. Fish are an important source of AMPs and, recently, we have isolated and characterized a new 22 amino acid residues peptide, the chionodracine (Cnd), from the Antarctic icefish Chionodraco hamatus. In this paper we focused on a new Cnd-derived mutant peptide, namely Cnd-m3a, designed to improve the selectivity against prokaryotic cells and the antimicrobial activity against human pathogens of the initial Cnd template. Cnd-m3a was used for immunization of rabbits, which gave rise to a polyclonal antibody able to detect the peptide. The interaction kinetic of Cnd-m3a with the Antarctic bacterium Psychrobacter sp. (TAD1) was imaged using a transmission electron microscopy (TEM) immunogold method. Initially the peptide was associated with the plasma membrane, but after 180 min of incubation, it was found in the cytoplasm interacting with a DNA target inside the bacterial cells. Using fluorescent probes we showed that the newly designed mutant can create pores in the outer membrane of the bacteria E. coli and Psychrobacter sp. (TAD1), confirming the results of TEM analysis. Moreover, in vitro assays demonstrated that Cnd-m3a is able to bind lipid vesicles of different compositions with a preference toward negatively charged ones, which mimics the prokaryotic cell. The Cnd-m3a peptide showed quite low hemolytic activity and weak cytotoxic effect against human primary and tumor cell lines, but high antimicrobial activity against selected Gram - human pathogens. These results highlighted the high potential of the Cnd-m3a peptide as a starting point for developing a new human therapeutic agent.
ISSN: 0145-305X
DOI: 10.1016/j.dci.2019.02.012
Appears in Collections:A1. Articolo in rivista

Files in This Item:
File Description SizeFormat Existing users please
1-s2.0-S0145305X1830630X-main.pdf2.51 MBAdobe PDF    Request a copy
Show full item record

Citations 5

Last Week
Last month
checked on Sep 20, 2021

Page view(s)

Last Week
Last month
checked on Sep 24, 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