ArticleBiophysical journal2016
Mode of Action of a Designed Antimicrobial Peptide: High Potency against Cryptococcus neoformans.
Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 42 citations in OpenAlex.
- The rise of ultrashort cationic β-peptides as promising antimicrobial therapeutics.RSC medicinal chemistry · 2025Review
- The Contribution of Human Antimicrobial Peptides to Fungi.International journal of molecular sciences · 2025Review
- Evaluation of proline-rich antimicrobial peptides as potential lead structures for novel antimycotics againstFrontiers in microbiology · 2023Article
- Atomic-Resolution Structures and Mode of Action of Clinically Relevant Antimicrobial Peptides.International journal of molecular sciences · 2022Review
- A Peptide from Budding Yeast GAPDH Serves as a Promising Antifungal against Cryptococcus neoformans.Microbiology spectrum · 2022Article
- In vitro Antifungal Activity of a Novel Antimicrobial Peptide AMP-17 Against Planktonic Cells and Biofilms ofInfection and drug resistance · 2022Article
- A saponin-polybromophenol antibiotic (CU1) fromCurrent research in pharmacology and drug discovery · 2022Article
- Fungicidal Activity of Recombinant Javanicin againstMolecules (Basel, Switzerland) · 2021Article
- A Novel Antimicrobial Peptide SparamosinFrontiers in microbiology · 2021Article
- Deuterium Solid State NMR Studies of Intact Bacteria Treated With Antimicrobial Peptides.Frontiers in medical technology · 2020Review
- Structural insights into the combinatorial effects of antimicrobial peptides reveal a role of aromatic-aromatic interactions in antibacterial synergism.The Journal of biological chemistry · 2019Article
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Corrections and comments
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Authors and funding
14 authors at 4 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
There is a significant need for developing compounds that kill Cryptococcus neoformans, the fungal pathogen that causes meningoencephalitis in immunocompromised individuals. Here, we report the mode of action of a designed antifungal peptide, VG16KRKP (VARGWKRKCPLFGKGG) against C. neoformans. It is shown that VG16KRKP kills fungal cells mainly through membrane compromise leading to efflux of ions and cell metabolites. Intracellular localization, inhibition of in vitro transcription, and DNA binding suggest a secondary mode of action for the peptide, hinting at possible intracellular targets. Atomistic structure of the peptide determined by NMR experiments on live C. neoformans cells reveals an amphipathic arrangement stabilized by hydrophobic interactions among A2, W5, and F12, a conventional folding pattern also known to play a major role in peptide-mediated Gram-negative bacterial killing, revealing the importance of this motif. These structural details in the context of live cell provide valuable insights into the design of potent peptides for effective treatment of human and plant fungal infections.
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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.