Spectroscopic study of antimicrobial peptides: Structure and functional activity

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 spec-troscopy. 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 inhi-bitory activities, were analyzed. (c) 2021 Elsevier B.V. All rights reserved.

Automated summary

Amphibians are a natural source of a variety of peptides with functional activities, which can be characterized using a complex of spectroscopic methods. The structure and functional activity of megin-1, a peptide isolated from amphibian skin, were studied using NMR, FTIR, CD, and UV-spectroscopy. Thermodynamic characteristics of peptide transformation and its antibacterial, antimycotic, and protease inhibitory activities were analyzed.