Brevinin-2GHk from Sylvirana guentheri and the design of truncated analogs exhibiting the enhancement of antimicrobial activity

Article


Chen, G., Miao, Y., Ma, C., Zhou, M., Shi, Z., Chen, X., Burrows, J., Xi, X., Chen, T. and Wang, L. 2020. Brevinin-2GHk from Sylvirana guentheri and the design of truncated analogs exhibiting the enhancement of antimicrobial activity. Antibiotics. 9 (2). https://doi.org/10.3390/antibiotics9020085
TypeArticle
TitleBrevinin-2GHk from Sylvirana guentheri and the design of truncated analogs exhibiting the enhancement of antimicrobial activity
AuthorsChen, G., Miao, Y., Ma, C., Zhou, M., Shi, Z., Chen, X., Burrows, J., Xi, X., Chen, T. and Wang, L.
Abstract

Brevinins are an important antimicrobial peptide (AMP) family discovered in the skin secretions of Ranidae frogs. The members demonstrate a typical C-terminal ranabox, as well as a diverse range of other structural characteristics. In this study, we identified a novel brevinin-2 peptide from the skin secretion of Sylvirana guentheri, via cloning transcripts, and identifying the expressed mature peptide, in the skin secretion. The confirmed amino acid sequence of the mature peptide was designated brevinin-2GHk (BR2GK). Moreover, as a previous study had demonstrated that the N-terminus of brevinin-2 is responsible for exerting antimicrobial activity, we also designed a series of truncated derivatives of BR2GK. The results show that the truncated derivatives exhibit significantly improved antimicrobial activity and cytotoxicity compared to the parent peptide, except a Pro14 substituted analog. The circular dichroism (CD) analysis of this analog revealed that it did not fold into a helical conformation in the presence of either lipopolysaccharides (LPS) or TFE, indicating that position 14 is involved in the formation of the α-helix. Furthermore, three more analogs with the substitutions of Ala, Lys and Arg at the position 14, respectively, revealed the influence on the membrane disruption potency on bacteria and mammalian cells by the structural changes at this position. Overall, the N-terminal 25-mer truncates demonstrated the potent antimicrobial activity with low cytotoxicity.

KeywordsAntimicrobial peptides, brevinin-2, frog skin secretion, truncated analogs
PublisherMDPI AG
JournalAntibiotics
ISSN2079-6382
Electronic2079-6382
Publication dates
Online14 Feb 2020
Print14 Feb 2020
Publication process dates
Deposited19 Feb 2020
Accepted12 Feb 2020
Output statusPublished
Publisher's version
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Copyright Statement

© 2020 by the authors.
Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license.

Additional information

This article belongs to the Special Issue Development of Antimicrobial Peptides from Amphibian

Digital Object Identifier (DOI)https://doi.org/10.3390/antibiotics9020085
LanguageEnglish
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