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.
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Schedule a callMore From: Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy
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