Spectroscopic study of antimicrobial peptides: Structure and functional activity

Polina Skvortsova; Yuliya Valiullina; Natalia Baranova; Dzhigangir Faizullin; Yuriy Zuev; Elena Ermakova

doi:10.1016/j.saa.2021.120273

Spectroscopic study of antimicrobial peptides: Structure and functional activity

Spectrochim Acta A Mol Biomol Spectrosc. 2022 Jan 5:264:120273. doi: 10.1016/j.saa.2021.120273. Epub 2021 Aug 12.

Authors

Polina Skvortsova¹, Yuliya Valiullina¹, Natalia Baranova¹, Dzhigangir Faizullin¹, Yuriy Zuev¹, Elena Ermakova²

Affiliations

¹ Kazan Institute of Biochemistry and Biophysics, FRC Kazan Scientific Center of RAS, Lobachevsky Str., 2/31, Kazan 420111, Russian Federation.
² Kazan Institute of Biochemistry and Biophysics, FRC Kazan Scientific Center of RAS, Lobachevsky Str., 2/31, Kazan 420111, Russian Federation. Electronic address: ermakova@kibb.knc.ru.

PMID: 34425316
DOI: 10.1016/j.saa.2021.120273

Abstract

Amphibians are a natural source of a large number of peptides with a wide range of functional activities. Here, a complex of spectroscopic methods including NMR-, FTIR-, CD-, and UV-spectroscopy was applied to characterize the structure and functional activity of megin-1, a peptide isolated from amphibian skin. The three-dimensional structure of two forms of the peptide was determined using solution NMR spectroscopy. Thermodynamic characteristics of the process of peptide transformation from linear to cyclic form were obtained. Antibacterial and antimycotic properties of the peptide, as well as its protease inhibitory activities, were analyzed.

Keywords: Antimicrobial activity; FTIR; NMR-spectroscopy; Three-dimensional structure.

MeSH terms

Anti-Bacterial Agents / pharmacology
Anti-Infective Agents* / pharmacology
Antimicrobial Cationic Peptides* / pharmacology
Magnetic Resonance Spectroscopy
Pore Forming Cytotoxic Proteins

Substances

Anti-Bacterial Agents
Anti-Infective Agents
Antimicrobial Cationic Peptides
Pore Forming Cytotoxic Proteins