5NGQ

Bicyclic antimicrobial peptides

Summary for 5NGQ

• Entry DOI: 10.2210/pdb5ngq/pdb
• Descriptor: Fucose-binding lectin II (PA-IIL), DLS-PRO-ALD-CYS-TYD-ALA-CYD-LYS-ALA, Fragment of bicycle, ... (6 entities in total)
• Functional Keywords: bycicle, antimicrobial peptide, pseudomonas aeruginosa, biofilm, sugar binding protein
• Biological source: Pseudomonas aeruginosa; More
• Total number of polymer chains: 8
• Total formula weight: 50727.67

Authors

Di Bonaventura, I.,Jin, X.,Visini, R.,Michaud, G.,Robadey, M.,Koehler, T.,van Delden, C.,Stocker, A.,Darbre, T.,Reymond, J.-L. (deposition date: 2017-03-20, release date: 2017-08-23, Last modification date: 2024-01-17)

Primary citation

Di Bonaventura, I.,Jin, X.,Visini, R.,Probst, D.,Javor, S.,Gan, B.H.,Michaud, G.,Natalello, A.,Doglia, S.M.,Kohler, T.,van Delden, C.,Stocker, A.,Darbre, T.,Reymond, J.L.
Chemical space guided discovery of antimicrobial bridged bicyclic peptides against Pseudomonas aeruginosa and its biofilms.
Chem Sci, 8:6784-6798, 2017

PubMed Abstract: Herein we report the discovery of antimicrobial bridged bicyclic peptides (AMBPs) active against , a highly problematic Gram negative bacterium in the hospital environment. Two of these AMBPs show strong biofilm inhibition and dispersal activity and enhance the activity of polymyxin, currently a last resort antibiotic against which resistance is emerging. To discover our AMBPs we used the concept of chemical space, which is well known in the area of small molecule drug discovery, to define a small number of test compounds for synthesis and experimental evaluation. Our chemical space was calculated using 2DP, a new topological shape and pharmacophore fingerprint for peptides. This method provides a general strategy to search for bioactive peptides with unusual topologies and expand the structural diversity of peptide-based drugs.

PubMed: 29147502
DOI: 10.1039/c7sc01314k

Experimental method

X-RAY DIFFRACTION (1.17 Å)