Matches in SemOpenAlex for { <https://semopenalex.org/work/W2535565146> ?p ?o ?g. }
- W2535565146 abstract "Peptide deformylase (PDF) is considered an excellent target to develop antibiotics. We have performed an extensive characterization of a new PDF from the pathogen Streptococcus agalactiae, showing properties similar to other known PDFs. S. agalactiae PDF could be used as PDF prototype as it allowed to get complete sets of 3-dimensional, biophysical and kinetic data with virtually any inhibitor compound. Structure-activity relationship analysis with this single reference system allowed us to reveal distinct binding modes for different PDF inhibitors and the key role of a hydrogen bond in potentiating the interaction between ligand and target. We propose this protein as an irreplaceable tool, allowing easy and relevant fine comparisons between series, to design, challenge and validate novel series of inhibitors. As proof-of-concept, we report here the design and synthesis of effective specific bacterial PDF inhibitors of an oxadiazole series with potent antimicrobial activity against a multidrug resistant clinical isolate." @default.
- W2535565146 created "2016-10-28" @default.
- W2535565146 creator A5015831996 @default.
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- W2535565146 creator A5090499815 @default.
- W2535565146 date "2016-10-20" @default.
- W2535565146 modified "2023-10-12" @default.
- W2535565146 title "A unique peptide deformylase platform to rationally design and challenge novel active compounds" @default.
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