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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Bibliographic Details
Published in:Toxins 2021-05, Vol.13 (5), p.343
Main Authors: Luo, Xudong, Ding, Li, Ye, Xiangdong, Zhu, Wen, Zhang, Kaiyue, Li, Fangyan, Jiang, Huiwen, Zhao, Zhiwen, Chen, Zongyun
Format: Article
Language:English
Subjects:
Amino acid sequence
Amino acids
Antibiotics
Antiinfectives and antibacterials
Antimicrobial activity
Antimicrobial agents
Antimicrobial peptides
antimicrobial resistance
Bacteria
Cytotoxicity
Design
Displays
Dosage
Drug development
Fluorescence
Gram-negative bacteria
Gram-positive bacteria
HeliQuest
Infectious diseases
Investigations
Iodides
Mammalian cells
noncysteine-containing AMPs
Peptides
Propidium iodide
Residues
scorpion venom
Smp43
Smp43(1-14)
Venom
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Summary: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, SYTOXTM Green and DiSC3-5, 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.
ISSN:2072-6651
2072-6651
DOI:10.3390/toxins13050343