Study on the structure-activity relationship of an antimicrobial peptide, Brevinin-2GUb, from the skin secretion of Hylarana guentheri

Lin, Yaxian, Liu, Siyan, Xi, Xinping, Ma, Chengbang, Wang, Lei ORCID: https://orcid.org/0000-0002-8811-8489, Chen, Xiaoling, Shi, Zhanzhong, Chen, Tianbao ORCID: https://orcid.org/0000-0001-8011-9260, Shaw, Chris and Zhou, Mei ORCID: https://orcid.org/0000-0003-2576-0252 (2021) Study on the structure-activity relationship of an antimicrobial peptide, Brevinin-2GUb, from the skin secretion of Hylarana guentheri. Antibiotics, 10 (8) , e895. ISSN 2079-6382 [Article] (doi:10.3390/antibiotics10080895)

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Abstract

Antimicrobial peptides (AMPs) are considered potential alternatives to antibiotics due to their advantages in solving antibiotic resistance. Brevinin-2GUb, which was extracted from the skin secretion of Hylarana guentheri, is a peptide with modest antimicrobial activity. Several analogues were designed to explore the structure–activity relationship and enhance its activity. In general, the Rana box is not an indispensable motif for the bioactivity of Brevinin-2GUb, and the first to the 19th amino acids at the N-terminal end are active fragments, such that shortening the peptide while maintaining its bioactivity is a promising strategy for the optimisation of peptides. Keeping a complete hydrophobic face and increasing the net charges are key factors for antimicrobial activity. With the increase of cationic charges, α-helical proportion, and amphipathicity, the activity of t-Brevinin-2GUb-6K (tB2U-6K), in combatting bacteria, drastically improved, especially against Gram-negative bacteria, and the peptide attained the capacity to kill clinical isolates and fungi as well, which made it possible to address some aspects of antibiotic resistance. Thus, peptide tB2U-6K, with potent antimicrobial activity against antibiotic-resistant bacteria, the capacity to inhibit the growth of biofilm, and low toxicity against normal cells, is of value to be further developed into an antimicrobial agent.

Item Type: Article
Additional Information: This article belongs to the Special Issue Natural Peptides from Arthropods, Amphibians, and Reptiles to Combat Conventional Antibiotic Resistance
Keywords (uncontrolled): antimicrobial peptides, Brevinin-2GUb, structure–activity relationship
Research Areas: A. > School of Science and Technology > Natural Sciences
Item ID: 33666
Notes on copyright: © 2021 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: 26 Jul 2021 15:24
Last Modified: 10 Sep 2021 09:56
URI: https://eprints.mdx.ac.uk/id/eprint/33666

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