5V1E
Suboptimization of a glycine rich peptide allows the combinatorial space exploration for designing novel antimicrobial peptides
Summary for 5V1E
| Entry DOI | 10.2210/pdb5v1e/pdb |
| NMR Information | BMRB: 30263 |
| Descriptor | Guavanin 2 (1 entity in total) |
| Functional Keywords | antibacterial, helix., antimicrobial protein |
| Biological source | synthetic construct |
| Total number of polymer chains | 1 |
| Total formula weight | 2648.08 |
| Authors | Alves, E.S.F.,Matos, C.O. (deposition date: 2017-03-02, release date: 2018-03-07, Last modification date: 2024-10-09) |
| Primary citation | Porto, W.F.,Irazazabal, L.,Alves, E.S.F.,Ribeiro, S.M.,Matos, C.O.,Pires, A.S.,Fensterseifer, I.C.M.,Miranda, V.J.,Haney, E.F.,Humblot, V.,Torres, M.D.T.,Hancock, R.E.W.,Liao, L.M.,Ladram, A.,Lu, T.K.,de la Fuente-Nunez, C.,Franco, O.L. In silico optimization of a guava antimicrobial peptide enables combinatorial exploration for peptide design. Nat Commun, 9:1490-1490, 2018 Cited by PubMed Abstract: Plants are extensively used in traditional medicine, and several plant antimicrobial peptides have been described as potential alternatives to conventional antibiotics. However, after more than four decades of research no plant antimicrobial peptide is currently used for treating bacterial infections, due to their length, post-translational modifications or high dose requirement for a therapeutic effect . Here we report the design of antimicrobial peptides derived from a guava glycine-rich peptide using a genetic algorithm. This approach yields guavanin peptides, arginine-rich α-helical peptides that possess an unusual hydrophobic counterpart mainly composed of tyrosine residues. Guavanin 2 is characterized as a prototype peptide in terms of structure and activity. Nuclear magnetic resonance analysis indicates that the peptide adopts an α-helical structure in hydrophobic environments. Guavanin 2 is bactericidal at low concentrations, causing membrane disruption and triggering hyperpolarization. This computational approach for the exploration of natural products could be used to design effective peptide antibiotics. PubMed: 29662055DOI: 10.1038/s41467-018-03746-3 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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