Conformational study of melectin and antapin antimicrobial peptides in model membrane environments

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61388963%3A_____%2F17%3A00475296" target="_blank" >RIV/61388963:_____/17:00475296 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/60461373:22320/17:43913252 RIV/60461373:22340/17:43913252

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.saa.2016.07.015" target="_blank" >http://dx.doi.org/10.1016/j.saa.2016.07.015</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.saa.2016.07.015" target="_blank" >10.1016/j.saa.2016.07.015</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Conformational study of melectin and antapin antimicrobial peptides in model membrane environments

Popis výsledku v původním jazyce

Antimicrobial peptides have long been considered as promising compounds against drug-resistant pathogens. In this work, we studied the secondary structure of antimicrobial peptides melectin and antapin using electronic (ECD) and vibrational circular dichroism (VCD) spectroscopies that are sensitive to peptide secondary structures. The results from quantitative ECD spectral evaluation by Dichroweb and CDNN program and from the qualitative evaluation of the VCD spectra were compared. The antimicrobial activity of the selected peptides depends on their ability to adopt an amphipathic alpha-helical conformation on the surface of the bacterial membrane. Hence, solutions of different zwitterionic and negatively charged liposomes and micelles were used to mimic the eukaryotic and bacterial biological membranes. The results show a significant content of alpha-helical conformation in the solutions of negatively charged liposomes mimicking the bacterial membrane, thus correlating with the antimicrobial activity of the studied peptides. On the other hand in the solutions of zwitterionic liposomes used as models of the eukaryotic membranes, the fraction of alpha-helical conformation was lower, which corresponds with their moderate hemolytic activity.

Název v anglickém jazyce

Conformational study of melectin and antapin antimicrobial peptides in model membrane environments

Popis výsledku anglicky

Antimicrobial peptides have long been considered as promising compounds against drug-resistant pathogens. In this work, we studied the secondary structure of antimicrobial peptides melectin and antapin using electronic (ECD) and vibrational circular dichroism (VCD) spectroscopies that are sensitive to peptide secondary structures. The results from quantitative ECD spectral evaluation by Dichroweb and CDNN program and from the qualitative evaluation of the VCD spectra were compared. The antimicrobial activity of the selected peptides depends on their ability to adopt an amphipathic alpha-helical conformation on the surface of the bacterial membrane. Hence, solutions of different zwitterionic and negatively charged liposomes and micelles were used to mimic the eukaryotic and bacterial biological membranes. The results show a significant content of alpha-helical conformation in the solutions of negatively charged liposomes mimicking the bacterial membrane, thus correlating with the antimicrobial activity of the studied peptides. On the other hand in the solutions of zwitterionic liposomes used as models of the eukaryotic membranes, the fraction of alpha-helical conformation was lower, which corresponds with their moderate hemolytic activity.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10406 - Analytical chemistry

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2017

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy

ISSN

1386-1425

e-ISSN

—

Svazek periodika

170

Číslo periodika v rámci svazku

Jan 5

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

9

Strana od-do

247-255

Kód UT WoS článku

000398746600033

EID výsledku v databázi Scopus

2-s2.0-84978405312