1. Brevinin-2PN, an antimicrobial peptide identified from dark-spotted frog (Pelophylax nigromaculatus), exhibits wound-healing activity.
- Author
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Fan XL, Yu SS, Zhao JL, Li Y, Zhan DJ, Xu F, Lin ZH, and Chen J
- Subjects
- Amino Acid Sequence, Animals, Anti-Bacterial Agents metabolism, Antimicrobial Cationic Peptides metabolism, Anura genetics, DNA, Complementary metabolism, Humans, Protein Sorting Signals, Ranidae genetics, Skin metabolism, Amphibian Proteins genetics, Amphibian Proteins metabolism, Antimicrobial Peptides
- Abstract
Brevinins exhibit a wide range of structural features and strong biological activities. Brevinin-2, derived from several amphibians, has shown antimicrobial activities. However, little is known about the wound-healing activity of brevinin-2. In this study, brevinin-2 cDNA was identified from the skin transcriptome of the dark-spotted frog (Pelophylax nigromaculatus) and it comprises a signal peptide, a propeptide, and a mature peptide. Sequence alignment with brevinin-2 derived from other amphibians showed variability of the mature peptide, and the presence of a C-terminal cyclic heptapeptide domain (Cys-Lys-Xaa4-Cys) in the mature peptide. Dark-spotted frog brevinin-2 belonged to the brevinin-2 cluster and was closely related to brevinin-2HB1 from Pelophylax hubeiensis. Synthetic dark-spotted frog brevinin-2 mature peptide (brevinin-2PN) exhibited antibacterial activity against several pathogens by destroying cell membrane integrity and hydrolysis of genomic DNA. Brevinin-2PN exhibited significant wound-healing activity by accelerating the healing of human skin fibroblast cell scratches, influencing cell migration, and stimulating gene expression of growth factors., (Copyright © 2022 Elsevier Ltd. All rights reserved.)
- Published
- 2022
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