ArticleScientific reports2017
Cathelicidin-trypsin inhibitor loop conjugate represents a promising antibiotic candidate with protease stability.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers, 1 of them a synthesis that pooled it.
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Who cites it
11 citing papers in PubMed, 1 synthesis or guideline pooled it, 26 citations in OpenAlex.
- Antibacterial action mechanisms and mode of trypsin inhibitors: a systematic review.Journal of enzyme inhibition and medicinal chemistry · 2022Pooled it
- Design of TAT-Conjugated Bowman-Birk Trypsin Inhibitor Peptides with Enhanced Antimicrobial and Antiproliferative Activities.Biomolecules · 2026Article
- Effect of trypsin inhibitor isolated from tamarind seed (TTI) on caenorhabditis elegans survival under bacterial infection.Journal of enzyme inhibition and medicinal chemistry · 2025Article
- Cathelicidin AS-12W Derived from the Alligator sinensis and Its Antimicrobial Activity Against Drug-Resistant Gram-Negative Bacteria In Vitro and In Vivo.Probiotics and antimicrobial proteins · 2025Article
- Piggybacking on nature: exploring the multifaceted world of porcine β-defensins.Veterinary research · 2025Review
- Antimicrobial property ofFood science & nutrition · 2022Article
- Potent antibacterial and antibiofilm activities of TICbf-14, a peptide with increased stability against trypsin.Journal of microbiology (Seoul, Korea) · 2022Article
- The Impact of Lung Proteases on Snake-Derived Antimicrobial Peptides.Biomolecules · 2021Article
- Potent antibacterial activity of MSI-1 derived from the magainin 2 peptide against drug-resistant bacteria.Theranostics · 2020Article
- Article
- Design and Assessment of Anti-Biofilm Peptides: Steps Toward Clinical Application.Journal of innate immunity · 2019Review
Corrections and comments
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Authors and funding
9 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cathelicidins are regarded as promising antibiotics due to their capability against antibiotic-resistant bacteria without cytotoxicity. However, some concerns about the balance of cytotoxicity and antimicrobial activity, weak stability and enzymatic susceptibility sually restrict their therapeutic use. Here, we designed a series of shortened variants, Hc1~15, based on our previously characterized Hc-CATH. Hc3, the one with the best activity, after point mutation was engineered with a trypsin inhibitor loop, ORB-C, to obtain four hybrid peptides: H3TI, TIH3, H3TIF and TIH3F. All four except TIH3 were found possessing an appreciable profile of proteases inhibitory and antimicrobial characteristics without increase in cytotoxicity. Among them, TIH3F exhibited the most potent and broad-spectrum antimicrobial and anti-inflammatory activities. Fluorescence spectroscopy has demonstrated a quick induction of bacterial membrane permeability by TIH3F leading to the cell death, which also accounts for its fast anti-biofilm activity. Such mode of antimicrobial action was mainly attributed to peptides' amphiphilic and helical structures determined by CD and homology modeling. Besides, TIH3F exhibited good tolerance to salt, serum, pH, and temperature, indicating a much better physiological stability in vitro than Hc3, Most importantly, in the case of resistance against proteases hydrolysis, current hybrid peptides displayed a remarkable enhancement than their original templates.
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