ArticleACS bio & med chem Au2025
Augmentation of Antimicrobial Activity of Spiniferin by Introducing an Arginine Residue Toward Its Amino Terminus: A Possible Role of Cation-π Interaction.
Article in ACS bio & med chem Au, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
0 citing papers in PubMed.
No citing paper in PubMed yet.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Spiniferin is a 13-mer scorpion-origin antimicrobial peptide having poor antimicrobial activity. To augment Spiniferin's antimicrobial activity, we enhanced its net positive charge by replacing a glutamic acid residue with an arginine residue toward its amino terminus. We envisaged that a cation-π interaction could be introduced between this arginine residue and the tryptophan residue located near the middle of Spiniferin. This cation-π interaction could promote stronger interaction of the peptide with a negatively charged bacterial membranes, resulting in its increased antimicrobial activity. Though glutamic acid-to-arginine substitution [Spiniferin-(E4R)] enhanced both the antimicrobial and toxic properties of Spiniferin, the same replacement with a d-arginine residue [Spiniferin-(E4dR)] significantly enhanced its antimicrobial activity against selected Gram-negative/positive bacteria and a MRSA strain while maintaining low hemolytic/cytotoxic properties. Interestingly, Spiniferin-(E4dR) analogs, with its aromatic-tryptophan residue substituted with an aromatic phenylalanine or an aliphatic valine residue, and its d-arginine residue replaced with a d-lysine residue, showed much lesser antibacterial activity than Spiniferin-(E4dR) or Spiniferin-(E4R). The results indicated a crucial role of the tryptophan and l-/d-arginine combination in augmenting the antimicrobial activity of Spiniferin analogs, Spiniferin-(E4R) and Spiniferin-(E4dR). Spiniferin-(E4dR) showed bactericidal properties against selected Gram-positive/negative bacteria. It permeabilized bacterial membranes and induced damages in bacterial membrane organization, suggesting that the bacterial plasma membrane is its target for exhibiting antimicrobial activity. Further, Spiniferin-(E4dR) in the intravenous route demonstrated the survival of E. coli ATCC 25922-infected mice and the clearance of bacteria from the visceral organs of these mice. Computational studies showed the requisite distance between the arginine's cationic side chain and the π-electron site of the tryptophan residue for a possible intramolecular cation-π interaction in Spiniferin-(E4dR)/Spiniferin-(E4R).
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.