7JGX
Solution NMR structure of neuroVAL, a derived peptide from wasp
Summary for 7JGX
Entry DOI | 10.2210/pdb7jgx/pdb |
NMR Information | BMRB: 30775 |
Descriptor | neuroVAL derived peptide ILE-PHE-TRP-LEU-PHE-ARG-GLY-LYS-ALA-ASP-VAL-ALA-LEU-NH2 (1 entity in total) |
Functional Keywords | alpha-helical, antimicrobial, non-haemolytic., antimicrobial protein |
Biological source | Parachartergus fraternus |
Total number of polymer chains | 1 |
Total formula weight | 1535.85 |
Authors | Muller, J.A.I.,Craik, D.J.,Koehbach, J. (deposition date: 2020-07-20, release date: 2020-12-16, Last modification date: 2024-10-16) |
Primary citation | Muller, J.A.I.,Lawrence, N.,Chan, L.Y.,Harvey, P.J.,Elliott, A.G.,Blaskovich, M.A.T.,Goncalves, J.C.,Galante, P.,Mortari, M.R.,Toffoli-Kadri, M.C.,Koehbach, J.,Craik, D.J. Antimicrobial and Anticancer Properties of Synthetic Peptides Derived from the Wasp Parachartergus fraternus. Chembiochem, 22:1415-1423, 2021 Cited by PubMed Abstract: Agelaia-MPI and protonectin are antimicrobial peptides isolated from the wasp Parachartergus fraternus that show antimicrobial and neuroactive activities. Previously, two analogues of these peptides, neuroVAL and protonectin-F, were designed to reduce nonspecific toxicity and improve potency. Here, the three-dimensional structures of neuroVAL, protonectin and protonectin-F were determined by using circular dichroism and NMR spectroscopy. Antibacterial, antifungal, cytotoxic and hemolytic activities were tested for the parent peptides and analogues. All peptides showed moderate antimicrobial activity against Gram-positive bacteria, with agelaia-MPI being the most active. Protonectin and protonectin-F were found to be toxic to cancerous and noncancerous cell lines. Internalization experiments revealed that these peptides accumulate inside both cell types. By contrast, neuroVAL was nontoxic to all tested cells and was able to enter cells without accumulating. In summary, neuroVAL has potential as a nontoxic cell-penetrating peptide, while protonectin-F needs further modification to realize its potential as an antitumor peptide. PubMed: 33244888DOI: 10.1002/cbic.202000716 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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