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

Article


Lin, Y., Liu, S., Xi, X., Ma, C., Wang, L., Chen, X., Shi, Z., Chen, T., Shaw, C. and Zhou, M. 2021. Study on the structure-activity relationship of an antimicrobial peptide, Brevinin-2GUb, from the skin secretion of Hylarana guentheri. Antibiotics. 10 (8). https://doi.org/10.3390/antibiotics10080895
TypeArticle
TitleStudy on the structure-activity relationship of an antimicrobial peptide, Brevinin-2GUb, from the skin secretion of Hylarana guentheri
AuthorsLin, Y., Liu, S., Xi, X., Ma, C., Wang, L., Chen, X., Shi, Z., Chen, T., Shaw, C. and Zhou, M.
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.

Keywordsantimicrobial peptides, Brevinin-2GUb, structure–activity relationship
PublisherMDPI AG
JournalAntibiotics
ISSN2079-6382
Publication dates
Online22 Jul 2021
Print22 Jul 2021
Publication process dates
Deposited26 Jul 2021
Accepted21 Jul 2021
Output statusPublished
Publisher's version
License
Copyright Statement

© 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.

Additional information

This article belongs to the Special Issue Natural Peptides from Arthropods, Amphibians, and Reptiles to Combat Conventional Antibiotic Resistance

Digital Object Identifier (DOI)https://doi.org/10.3390/antibiotics10080895
LanguageEnglish
Permalink -

https://repository.mdx.ac.uk/item/89709

  • 47
    total views
  • 24
    total downloads
  • 0
    views this month
  • 0
    downloads this month

Export as

Related outputs

Broad-spectrum antimicrobial activity and improved stability of a D-Amino acid enantiomer of DMPC-10A, the designed derivative of dermaseptin truncates
Zai, Y., Ying, Y., Ye, Z., Zhou, M., Ma, C., Shi, Z., Chen, X., Xi, X., Chen, T. and Wang, L. 2020. Broad-spectrum antimicrobial activity and improved stability of a D-Amino acid enantiomer of DMPC-10A, the designed derivative of dermaseptin truncates. Antibiotics. 9 (9), pp. 1-19. https://doi.org/10.3390/antibiotics9090627
Brevinin-2GHk from Sylvirana guentheri and the design of truncated analogs exhibiting the enhancement of antimicrobial activity
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