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Titolo:
Metal compound-mediated hydrolytic cleavage of oxidized insulin B chain: Regioselectivity and influence of peptide secondary structure
Autore:
Luo, XM; He, WJ; Zhang, Y; Guo, ZJ; Zhu, LG;
Indirizzi:
Nanjing Univ, State Key Lab Coordinat Chem, Inst Coordinat Chem, Nanjing 210093, Jiangsu, Peoples R China Nanjing Univ Nanjing Jiangsu Peoples R China 210093 ngsu, Peoples R China
Titolo Testata:
CHINESE JOURNAL OF CHEMISTRY
fascicolo: 6, volume: 18, anno: 2000,
pagine: 855 - 862
SICI:
1001-604X(200011/12)18:6<855:MCHCOO>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
HISTIDINE-CONTAINING PEPTIDES; PALLADIUM(II) AQUA COMPLEXES; METHIONINE-CONTAINING DIPEPTIDES; PLATINUM(II) COMPLEXES; SELECTIVE HYDROLYSIS; COORDINATION; LIGANDS; BONDS; SUBSTITUTION; COPPER(II);
Keywords:
insulin B chain; hydrolytic cleavage; palladium(II); complexes; Cu(II) ion; electrospray mass spectrometry;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
33
Recensione:
Indirizzi per estratti:
Indirizzo: Zhu, LG Nanjing Univ, State Key Lab Coordinat Chem, Inst Coordinat Chem, Nanjing 210093, Jiangsu, Peoples R China Nanjing Univ Nanjing Jiangsu Peoples R China 210093 oples R China
Citazione:
X.M. Luo et al., "Metal compound-mediated hydrolytic cleavage of oxidized insulin B chain: Regioselectivity and influence of peptide secondary structure", CHIN J CHEM, 18(6), 2000, pp. 855-862

Abstract

The interaction of oxidized insulin B chain (B) with cis-[Pd(en)Cl-2] (en = ethylenediamine), cis-[Pd-(dtco-3-OH)Cl-2] (dtco-3-OH = dithiacyclooctan-3-ol) and CuCl2 was studied by electrospray mass spectrometry. It is discovered that the binding of Pd(II) complexes and the sites of cleavage are highly dependent on the secondary structure and local environment of B. The hydrolytic cleavage of denatured B by Pd(II) complexes was monitored by HPLC. The reaction is regioselective and follows first order kinetics with half-life of 4.8 days at 40 degreesC. Two amide bonds, i.e. at Leu6-Cys7 and at Gly8-Ser9, which are close to the two potential Pd(II) binding sites His5 and His10, are selectively cleaved. In the case of Cu(II) ion as promoter, only one cleavage site was observed which is located at Gly8-Ser9 bond. These results provide improved understanding on the design of artificial metallopeptidase.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 21/09/20 alle ore 12:44:48