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

Chen, Guanzhyu, Miao, Yuxi, Ma, Chengbang, Zhou, Mei, Shi, Zhanzhong, Chen, Xiaoling Chen, Burrows, James F., Xi, Xinping, Chen, Tianbao and Wang, Lei (2020) Brevinin-2GHk from Sylvirana guentheri and the design of truncated analogs exhibiting the enhancement of antimicrobial activity. Antibiotics, 9 (2) , e85. ISSN 2079-6382 [Article] (doi:10.3390/antibiotics9020085)

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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.

Item Type: Article
Additional Information: This article belongs to the Special Issue Development of Antimicrobial Peptides from Amphibian
Keywords (uncontrolled): Antimicrobial peptides, brevinin-2, frog skin secretion, truncated analogs
Research Areas: A. > School of Science and Technology > Natural Sciences
Item ID: 29091
Notes on copyright: © 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.
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Depositing User: Jisc Publications Router
Date Deposited: 19 Feb 2020 11:47
Last Modified: 09 Mar 2020 17:58

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