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Article

In Silico and In Vitro Structure–Activity Relationship of Mastoparan and Its Analogs

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Protein and Proteomics Research Center for Commercial and Industrial Purposes (ProCCI), Khon Kaen University, Khon Kaen 40002, Thailand
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Division of Pharmacognosy and Toxicology, Faculty of Pharmaceutical Sciences, Khon Kaen University, Khon Kaen 40002, Thailand
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Toxicology and Pharmacology, Campus Gasthuisberg, University of Leuven (KU Leuven), O&N 2, P.O. Box 922, Herestraat 49, 3000 Leuven, Belgium
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Department of Biochemistry, Faculty of Science, Khon Kaen University, Khon Kaen 40002, Thailand
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Authors to whom correspondence should be addressed.
Academic Editors: Sónia Silva, Daniele Castagnolo, Jürgen Brem and Mark G. Moloney
Molecules 2022, 27(2), 561; https://doi.org/10.3390/molecules27020561
Received: 10 December 2021 / Revised: 6 January 2022 / Accepted: 12 January 2022 / Published: 16 January 2022
Antimicrobial peptides are an important class of therapeutic agent used against a wide range of pathogens such as Gram-negative and Gram-positive bacteria, fungi, and viruses. Mastoparan (MpVT) is an α-helix and amphipathic tetradecapeptide obtained from Vespa tropica venom. This peptide exhibits antibacterial activity. In this work, we investigate the effect of amino acid substitutions and deletion of the first three C-terminal residues on the structure–activity relationship. In this in silico study, the predicted structure of MpVT and its analog have characteristic features of linear cationic peptides rich in hydrophobic and basic amino acids without disulfide bonds. The secondary structure and the biological activity of six designed analogs are studied. The biological activity assays show that the substitution of phenylalanine (MpVT1) results in a higher antibacterial activity than that of MpVT without increasing toxicity. The analogs with the first three deleted C-terminal residues showed decreased antibacterial and hemolytic activity. The CD (circular dichroism) spectra of these peptides show a high content α-helical conformation in the presence of 40% 2,2,2-trifluoroethanol (TFE). In conclusion, the first three C-terminal deletions reduced the length of the α-helix, explaining the decreased biological activity. MpVTs show that the hemolytic activity of mastoparan is correlated to mean hydrophobicity and mean hydrophobic moment. The position and spatial arrangement of specific hydrophobic residues on the non-polar face of α-helical AMPs may be crucial for the interaction of AMPs with cell membranes. View Full-Text
Keywords: mastoparan; antimicrobial peptides; hemolysis; circular dichroism; venom; wasp mastoparan; antimicrobial peptides; hemolysis; circular dichroism; venom; wasp
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MDPI and ACS Style

Rungsa, P.; Peigneur, S.; Jangpromma, N.; Klaynongsruang, S.; Tytgat, J.; Daduang, S. In Silico and In Vitro Structure–Activity Relationship of Mastoparan and Its Analogs. Molecules 2022, 27, 561. https://doi.org/10.3390/molecules27020561

AMA Style

Rungsa P, Peigneur S, Jangpromma N, Klaynongsruang S, Tytgat J, Daduang S. In Silico and In Vitro Structure–Activity Relationship of Mastoparan and Its Analogs. Molecules. 2022; 27(2):561. https://doi.org/10.3390/molecules27020561

Chicago/Turabian Style

Rungsa, Prapenpuksiri, Steve Peigneur, Nisachon Jangpromma, Sompong Klaynongsruang, Jan Tytgat, and Sakda Daduang. 2022. "In Silico and In Vitro Structure–Activity Relationship of Mastoparan and Its Analogs" Molecules 27, no. 2: 561. https://doi.org/10.3390/molecules27020561

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