ArticleScientific reports2017
Mechanistic and structural basis of bioengineered bovine Cathelicidin-5 with optimized therapeutic activity.
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 7 papers.
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Who cites it
7 citing papers in PubMed, 12 citations in OpenAlex.
- MA-PEP: A novel anticancer peptide prediction framework with multimodal feature fusion based on attention mechanism.Protein science : a publication of the Protein Society · 2024Article
- Synthetic antimicrobial peptides Bac-5, BMAP-28, and Syn-1 can inhibit bovine respiratory disease pathogensFrontiers in veterinary science · 2024Article
- Lessons from a Single Amino Acid Substitution: Anticancer and Antibacterial Properties of Two Phospholipase ACurrent issues in molecular biology · 2021Article
- Significance of Endogenous Antimicrobial Peptides on the Health of Food Animals.Frontiers in veterinary science · 2021Review
- Gadolinium Complexes as Contrast Agent for Cellular NMR Spectroscopy.International journal of molecular sciences · 2020Article
- Diverse Structural Conversion and Aggregation Pathways of Alzheimer's Amyloid-β (1-40).ACS nano · 2019Article
- BeStSel: a web server for accurate protein secondary structure prediction and fold recognition from the circular dichroism spectra.Nucleic acids research · 2018Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Peptide-drug discovery using host-defense peptides becomes promising against antibiotic-resistant pathogens and cancer cells. Here, we customized the therapeutic activity of bovine cathelicidin-5 targeting to bacteria, protozoa, and tumor cells. The membrane dependent conformational adaptability and plasticity of cathelicidin-5 is revealed by biophysical analysis and atomistic simulations over 200 μs in thymocytes, leukemia, and E. coli cell-membranes. Our understanding of energy-dependent cathelicidin-5 intrusion in heterogeneous membranes aided in designing novel loss/gain-of-function analogues. In vitro findings identified leucine-zipper to phenylalanine substitution in cathelicidin-5 (1-18) significantly enhance the antimicrobial and anticancer activity with trivial hemolytic activity. Targeted mutants of cathelicidin-5 at kink region and N-terminal truncation revealed loss-of-function. We ensured the existence of a bimodal mechanism of peptide action (membranolytic and non-membranolytic) in vitro. The melanoma mouse model in vivo study further supports the in vitro findings. This is the first structural report on cathelicidin-5 and our findings revealed potent therapeutic application of designed cathelicidin-5 analogues.
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