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An Smp43-Derived Short-Chain α-Helical Peptide Displays a Unique Sequence and Possesses Antimicrobial Activity against Both Gram-Positive and Gram-Negative Bacteria

Scorpion venoms are rich resources of antimicrobial peptides (AMPs). While the short-chain noncysteine-containing AMPs have attracted much attention as templates for drug development, the antimicrobial potential of long-chain noncysteine-containing AMPs has been largely overlooked. Here, by using th...

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Autores principales: Luo, Xudong, Ding, Li, Ye, Xiangdong, Zhu, Wen, Zhang, Kaiyue, Li, Fangyan, Jiang, Huiwen, Zhao, Zhiwen, Chen, Zongyun
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8150835/
https://www.ncbi.nlm.nih.gov/pubmed/34064808
http://dx.doi.org/10.3390/toxins13050343
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author Luo, Xudong
Ding, Li
Ye, Xiangdong
Zhu, Wen
Zhang, Kaiyue
Li, Fangyan
Jiang, Huiwen
Zhao, Zhiwen
Chen, Zongyun
author_facet Luo, Xudong
Ding, Li
Ye, Xiangdong
Zhu, Wen
Zhang, Kaiyue
Li, Fangyan
Jiang, Huiwen
Zhao, Zhiwen
Chen, Zongyun
author_sort Luo, Xudong
collection PubMed
description Scorpion venoms are rich resources of antimicrobial peptides (AMPs). While the short-chain noncysteine-containing AMPs have attracted much attention as templates for drug development, the antimicrobial potential of long-chain noncysteine-containing AMPs has been largely overlooked. Here, by using the online HeliQuest server, we designed and analyzed a series of 14-residue fragments of Smp43, a 43-residue long-chain noncysteine-containing AMP identified from the venom of Scorpio maurus palmatus. We found that Smp43(1-14) shows high antimicrobial activity against both Gram-positive and Gram-negative bacteria and is nontoxic to mammalian cells at the antimicrobial dosage. Sequence alignments showed that the designed Smp43(1-14) displays a unique primary structure that is different from other natural short-chain noncysteine-containing AMPs from scorpions, such as Uy17, Uy192 and IsCT. Moreover, the peptide Smp43(1-14) caused concentration-dependent fluorescence increases in the bacteria for all of the tested dyes, propidium iodide, SYTOX(TM) Green and DiSC(3)-5, suggesting that the peptide may kill the bacteria through the formation of pore structures in the plasma membrane. Taken together, our work sheds light on a new avenue for the design of novel short-chain noncysteine-containing AMPs and provides a good peptide template with a unique sequence for the development of novel drugs for use against bacterial infectious diseases.
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spelling pubmed-81508352021-05-27 An Smp43-Derived Short-Chain α-Helical Peptide Displays a Unique Sequence and Possesses Antimicrobial Activity against Both Gram-Positive and Gram-Negative Bacteria Luo, Xudong Ding, Li Ye, Xiangdong Zhu, Wen Zhang, Kaiyue Li, Fangyan Jiang, Huiwen Zhao, Zhiwen Chen, Zongyun Toxins (Basel) Article Scorpion venoms are rich resources of antimicrobial peptides (AMPs). While the short-chain noncysteine-containing AMPs have attracted much attention as templates for drug development, the antimicrobial potential of long-chain noncysteine-containing AMPs has been largely overlooked. Here, by using the online HeliQuest server, we designed and analyzed a series of 14-residue fragments of Smp43, a 43-residue long-chain noncysteine-containing AMP identified from the venom of Scorpio maurus palmatus. We found that Smp43(1-14) shows high antimicrobial activity against both Gram-positive and Gram-negative bacteria and is nontoxic to mammalian cells at the antimicrobial dosage. Sequence alignments showed that the designed Smp43(1-14) displays a unique primary structure that is different from other natural short-chain noncysteine-containing AMPs from scorpions, such as Uy17, Uy192 and IsCT. Moreover, the peptide Smp43(1-14) caused concentration-dependent fluorescence increases in the bacteria for all of the tested dyes, propidium iodide, SYTOX(TM) Green and DiSC(3)-5, suggesting that the peptide may kill the bacteria through the formation of pore structures in the plasma membrane. Taken together, our work sheds light on a new avenue for the design of novel short-chain noncysteine-containing AMPs and provides a good peptide template with a unique sequence for the development of novel drugs for use against bacterial infectious diseases. MDPI 2021-05-11 /pmc/articles/PMC8150835/ /pubmed/34064808 http://dx.doi.org/10.3390/toxins13050343 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/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 (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Article
Luo, Xudong
Ding, Li
Ye, Xiangdong
Zhu, Wen
Zhang, Kaiyue
Li, Fangyan
Jiang, Huiwen
Zhao, Zhiwen
Chen, Zongyun
An Smp43-Derived Short-Chain α-Helical Peptide Displays a Unique Sequence and Possesses Antimicrobial Activity against Both Gram-Positive and Gram-Negative Bacteria
title An Smp43-Derived Short-Chain α-Helical Peptide Displays a Unique Sequence and Possesses Antimicrobial Activity against Both Gram-Positive and Gram-Negative Bacteria
title_full An Smp43-Derived Short-Chain α-Helical Peptide Displays a Unique Sequence and Possesses Antimicrobial Activity against Both Gram-Positive and Gram-Negative Bacteria
title_fullStr An Smp43-Derived Short-Chain α-Helical Peptide Displays a Unique Sequence and Possesses Antimicrobial Activity against Both Gram-Positive and Gram-Negative Bacteria
title_full_unstemmed An Smp43-Derived Short-Chain α-Helical Peptide Displays a Unique Sequence and Possesses Antimicrobial Activity against Both Gram-Positive and Gram-Negative Bacteria
title_short An Smp43-Derived Short-Chain α-Helical Peptide Displays a Unique Sequence and Possesses Antimicrobial Activity against Both Gram-Positive and Gram-Negative Bacteria
title_sort smp43-derived short-chain α-helical peptide displays a unique sequence and possesses antimicrobial activity against both gram-positive and gram-negative bacteria
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8150835/
https://www.ncbi.nlm.nih.gov/pubmed/34064808
http://dx.doi.org/10.3390/toxins13050343
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