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Titolo:
Interaction of coumarin derivatives with human serum albumin: investigation by fluorescence spectroscopic technique and modeling studies
Autore:
Shobini, J; Mishra, AK; Sandhya, K; Chandra, N;
Indirizzi:
Indian Inst Technol, Dept Chem, Chennai 600036, India Indian Inst TechnolChennai India 600036 ept Chem, Chennai 600036, India NIMHANS, Dept Psychopharmacol, Bangalore, Karnataka, India NIMHANS Bangalore Karnataka India pharmacol, Bangalore, Karnataka, India Indian Inst Sci, Bioinformat Ctr, Bangalore 560012, Karnataka, India Indian Inst Sci Bangalore Karnataka India 560012 560012, Karnataka, India
Titolo Testata:
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
fascicolo: 5, volume: 57, anno: 2001,
pagine: 1133 - 1147
SICI:
1386-1425(200104)57:5<1133:IOCDWH>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
DRUG-BINDING-SITES; BENZODIAZEPINE BINDING; CHARGE-TRANSFER; DYNAMICS; ACIDS;
Keywords:
human serum albumin; coumarin; modeling; docking; binding site;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
31
Recensione:
Indirizzi per estratti:
Indirizzo: Mishra, AK Indian Inst Technol, Dept Chem, Chennai 600036, India Indian Inst Technol Chennai India 600036 hennai 600036, India
Citazione:
J. Shobini et al., "Interaction of coumarin derivatives with human serum albumin: investigation by fluorescence spectroscopic technique and modeling studies", SPECT ACT A, 57(5), 2001, pp. 1133-1147

Abstract

Interactions of several 7-aminocoumarins with human serum albumin (HSA) were studied by using fluorescence spectroscopic technique and modeling studies. There is a large change in fluorescence spectral parameters like intensity, emission maxima and anisotropy for all aminocoumarins. There were two binding sites for cou-1, 311 and a single binding site for other coumarins. The binding constant(s) are large for all coumarins reflective of a strongbinding. These spectral studies show that structural variants at the third, fourth and seventh position affects binding. The probable location of these coumarins in domain Ii has been predicted based on modeling. The effect of structural modification on the efficiency of binding was obtained for various other coumarins, using modeling. (C) 2001 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 18/01/20 alle ore 07:28:08