title: Zinc binding in peptide models of angiotensin-I converting enzyme active sites studied through 1H-NMR and chemical shift perturbation mapping.
abstract: We report the design and synthesis through solid phase 9-flourenylmethoxycarbonyl (Fmoc) chemistry of the two angiotensin-I converting enzyme active sites possessing the general sequence HEMGHX(23)EAIGDX(3). Their zinc-binding properties were monitored in solution through high-resolution (1)H-NMR. The obtained data were analyzed in terms of chemical shift differences. The results indicate that zinc binds to the HEMGH and the EAIGD characteristic motifs, and suggest possible coordination modes of zinc in the native enzyme.
authors.affiliation: Department of Pharmacy, University of Patras, GR-26500, Patras, Greece.
authors.forename: Athanassios S
authors.initials: AS
authors.lastname: Galanis
authors.forename: Georgios A
authors.initials: GA
authors.lastname: Spyroulias
authors.forename: Roberta
authors.initials: R
authors.lastname: Pierattelli
authors.forename: Andreas
authors.initials: A
authors.lastname: Tzakos
authors.forename: Anastassios
authors.initials: A
authors.lastname: Troganis
authors.forename: Ioannis P
authors.initials: IP
authors.lastname: Gerothanassis
authors.forename: George
authors.initials: G
authors.lastname: Pairas
authors.forename: Evy
authors.initials: E
authors.lastname: Manessi-Zoupa
authors.forename: Paul
authors.initials: P
authors.lastname: Cordopatis
mesh_terms: D020816:Amino Acid Motifs; D000595:Amino Acid Sequence; D001665:Binding Sites; D006801:Humans; D007527:Isoenzymes / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000737:chemistry / Q000378:metabolism; D010449:Peptide Mapping; D007703:Peptidyl-Dipeptidase A / Q000737:chemistry* / Q000378:metabolism*; D011487:Protein Conformation; D011522:Protons; D017386:Sequence Homology, Amino Acid; D012996:Solutions; D013820:Thermolysin / Q000737:chemistry / Q000378:metabolism; D015032:Zinc / Q000378:metabolism*
chemical_list: D007527:Isoenzymes; D010446:Peptide Fragments; D011522:Protons; D012996:Solutions; D007703:Peptidyl-Dipeptidase A; D013820:Thermolysin; D015032:Zinc