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
Type | Article |
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Title | Brevinin-2GHk from Sylvirana guentheri and the design of truncated analogs exhibiting the enhancement of antimicrobial activity |
Authors | Chen, 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. |
Keywords | Antimicrobial peptides, brevinin-2, frog skin secretion, truncated analogs |
Publisher | MDPI AG |
Journal | Antibiotics |
ISSN | 2079-6382 |
Electronic | 2079-6382 |
Publication dates | |
Online | 14 Feb 2020 |
14 Feb 2020 | |
Publication process dates | |
Deposited | 19 Feb 2020 |
Accepted | 12 Feb 2020 |
Output status | Published |
Publisher's version | License |
Copyright Statement | © 2020 by the authors. |
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 |
Language | English |
https://repository.mdx.ac.uk/item/88wq1
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