title: Dynamic combinatorial mass spectrometry leads to metallo-beta-lactamase inhibitors.
abstract: The use of protein ESI mass spectrometry under non-denaturing conditions to analyze a dynamic combinatorial library of thiols/disulfides with the BcII metallo-beta-lactamase enabled the rapid identification of an inhibitor with a K(i) of < 1 microM. The study exemplifies the utility of protein-MS for screening dynamic mixtures of potential enzyme-inhibitors.
authors.affiliation: Chemistry Research Laboratory and OCISB, Oxford, UK.
authors.forename: Benoît M R
authors.initials: BM
authors.lastname: Liénard
authors.forename: Rebekka
authors.initials: R
authors.lastname: Hüting
authors.forename: Patricia
authors.initials: P
authors.lastname: Lassaux
authors.forename: Moreno
authors.initials: M
authors.lastname: Galleni
authors.forename: Jean-Marie
authors.initials: JM
authors.lastname: Frère
authors.forename: Christopher J
authors.initials: CJ
authors.lastname: Schofield
mesh_terms: D007700:Kinetics; D008958:Models, Molecular; D021241:Spectrometry, Mass, Electrospray Ionization; D013329:Structure-Activity Relationship; D013438:Sulfhydryl Compounds / Q000138:chemical synthesis* / Q000737:chemistry; D065093:beta-Lactamase Inhibitors; D001618:beta-Lactamases / Q000737:chemistry*
chemical_list: D013438:Sulfhydryl Compounds; D065093:beta-Lactamase Inhibitors; C455979:beta-lactamase BcII; D001618:beta-Lactamases