ArticleScientific reports2015
An unprecedented alteration in mode of action of IsCT resulting its translocation into bacterial cytoplasm and inhibition of macromolecular syntheses.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Engineering the Host Defense Peptide from Scorpion Venom for Safer and More Potent Antibreast Cancer Activity.ACS pharmacology & translational science · 2026Article
- Designing a Potent, Low-Toxicity Antimicrobial Peptide Inspired by Scorpion Peptides: Optimizing Expression and Activity.Probiotics and antimicrobial proteins · 2026Article
- Experimental screening and structure-informed engineering of peptide-fused bacteriophage lysins with enhanced activity against Gram-negative bacteria.Frontiers in pharmacology · 2026Article
- Augmentation of Antimicrobial Activity of Spiniferin by Introducing an Arginine Residue Toward Its Amino Terminus: A Possible Role of Cation-π Interaction.ACS bio & med chem Au · 2025Article
- Endolysins as Effective Agents for DecontaminatingInternational journal of molecular sciences · 2025Article
- Antitumoral and Antiproliferative Potential of Synthetic Derivatives of Scorpion Peptide IsCT1 in an Oral Cavity Squamous Carcinoma Model.Molecules (Basel, Switzerland) · 2024Article
- Anti-Biofilm and Anti-Inflammatory Properties of the Truncated Analogs of the Scorpion Venom-Derived Peptide IsCT againstAntibiotics (Basel, Switzerland) · 2024Article
- Short-Chained Linear Scorpion Peptides: A Pool for Novel Antimicrobials.Antibiotics (Basel, Switzerland) · 2024Review
- Short Antimicrobial Peptide Derived from the Venom Gland Transcriptome ofAntibiotics (Basel, Switzerland) · 2023Article
- Antimicrobial Peptide Analogs From Scorpions: Modifications and Structure-Activity.Frontiers in molecular biosciences · 2022Review
- Antibacterial Activity and Toxicity of Analogs of Scorpion Venom IsCT Peptides.Antibiotics (Basel, Switzerland) · 2017Article
- Identification of GXXXXG motif in Chrysophsin-1 and its implication in the design of analogs with cell-selective antimicrobial and anti-endotoxin activities.Scientific reports · 2017Article
- Piscidin-1-analogs with double L- and D-lysine residues exhibited different conformations in lipopolysaccharide but comparable anti-endotoxin activities.Scientific reports · 2017Article
- Single Amino Acid Substitutions at Specific Positions of the Heptad Repeat Sequence of Piscidin-1 Yielded Novel Analogs That Show Low Cytotoxicity and In Vitro and In Vivo Antiendotoxin Activity.Antimicrobial agents and chemotherapy · 2016Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
IsCT, a 13-residue, non-cell-selective antimicrobial peptide is comprised of mostly hydrophobic residues and lesser cationic residues. Assuming that placement of an additional positive charge in the non-polar face of IsCT could reduce its hydrophobic interaction, resulting in its reduction of cytotoxicity, an analog, I9K-IsCT was designed. Two more analogs, namely, E7K-IsCT and E7K,I9K-IsCT, were designed to investigate the impact of positive charges in the polar face as well as polar and non-polar faces at a time. These amino acid substitutions resulted in a significant enhancement of therapeutic potential of IsCT. IsCT and E7K-IsCT seem to target bacterial membrane for their anti-bacterial activity. However, I9K-IsCT and E7K,I9K-IsCT inhibited nucleic acid and protein syntheses in tested E. coli without perturbing its membrane. This was further supported by the observation that NBD-IsCT localized onto bacterial membrane while NBD-labeled I9K-IsCT and E7K,I9K-IsCT translocated into bacterial cytoplasm. Interestingly, IsCT and E7K-IsCT were significantly helical while I9K-IsCT and E7K,I9K-IsCT were mostly unstructured with no helix content in presence of mammalian and bacterial membrane-mimetic lipid vesicles. Altogether, the results identify two novel cell-selective analogs of IsCT with new prototype amino acid sequences that can translocate into bacterial cytoplasm without any helical structure and inhibit macromolecular syntheses.
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