Next Article in Journal
Aspalathin-Enriched Green Rooibos Extract Reduces Hepatic Insulin Resistance by Modulating PI3K/AKT and AMPK Pathways
Next Article in Special Issue
Synthesis, Characterization, and Bacterial Fouling-Resistance Properties of Polyethylene Glycol-Grafted Polyurethane Elastomers
Previous Article in Journal
Sulforaphane Protect Against Cadmium-Induced Oxidative Damage in mouse Leydigs Cells by Activating Nrf2/ARE Signaling Pathway
Previous Article in Special Issue
Functionalized Polymeric Materials with Bio-Derived Antimicrobial Peptides for “Active” Packaging
Article Menu
Issue 3 (February-1) cover image

Export Article

Open AccessArticle

Interaction of Halictine-Related Antimicrobial Peptides with Membrane Models

1
Institute of Physics, Faculty of Mathematics and Physics, Charles University, Ke Karlovu 5, 121 16 Prague 2, Czech Republic
2
Institute of Organic Chemistry and Biochemistry, v.v.i., Academy of Sciences of the Czech Republic, Flemingovo náměstí 2, 166 10 Prague 6, Czech Republic
*
Author to whom correspondence should be addressed.
Int. J. Mol. Sci. 2019, 20(3), 631; https://doi.org/10.3390/ijms20030631
Received: 27 December 2018 / Revised: 24 January 2019 / Accepted: 28 January 2019 / Published: 1 February 2019
(This article belongs to the Special Issue Polymeric Systems as Antimicrobial or Antifouling Agents)
  |  
PDF [5428 KB, uploaded 1 February 2019]
  |  

Abstract

We have investigated structural changes of peptides related to antimicrobial peptide Halictine-1 (HAL-1) induced by interaction with various membrane-mimicking models with the aim to identify a mechanism of the peptide mode of action and to find a correlation between changes of primary/secondary structure and biological activity. Modifications in the HAL-1 amino acid sequence at particular positions, causing an increase of amphipathicity (Arg/Lys exchange), restricted mobility (insertion of Pro) and consequent changes in antimicrobial and hemolytic activity, led to different behavior towards model membranes. Secondary structure changes induced by peptide-membrane interaction were studied by circular dichroism, infrared spectroscopy, and fluorescence spectroscopy. The experimental results were complemented by molecular dynamics calculations. An α-helical structure has been found to be necessary but not completely sufficient for the HAL-1 peptides antimicrobial action. The role of alternative conformations (such as β-sheet, PPII or 310-helix) also seems to be important. A mechanism of the peptide mode of action probably involves formation of peptide assemblies (possibly membrane pores), which disrupt bacterial membrane and, consequently, allow membrane penetration. View Full-Text
Keywords: antibacterial peptides; halictine; circular dichroism; fluorescence; infrared spectroscopy antibacterial peptides; halictine; circular dichroism; fluorescence; infrared spectroscopy
Figures

Graphical abstract

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited (CC BY 4.0).
SciFeed

Share & Cite This Article

MDPI and ACS Style

Pazderková, M.; Maloň, P.; Zíma, V.; Hofbauerová, K.; Kopecký, V., Jr.; Kočišová, E.; Pazderka, T.; Čeřovský, V.; Bednárová, L. Interaction of Halictine-Related Antimicrobial Peptides with Membrane Models. Int. J. Mol. Sci. 2019, 20, 631.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Int. J. Mol. Sci. EISSN 1422-0067 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top