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Titolo:
Interaction of hypericin with serum albumins: Surface-enhanced Raman spectroscopy, resonance Raman spectroscopy and molecular modeling study
Autore:
Miskovsky, P; Hritz, J; Sanchez-Cortes, S; Fabriciova, F; Ulicny, J; Chinsky, L;
Indirizzi:
Safarik Univ, Dept Biophys, Kosice 04154, Slovakia Safarik Univ Kosice Slovakia 04154 Dept Biophys, Kosice 04154, Slovakia Ctr Int Laser, Bratislava, Slovakia Ctr Int Laser Bratislava SlovakiaCtr Int Laser, Bratislava, Slovakia CSIC, Inst Estructura Mat, E-28006 Madrid, Spain CSIC Madrid Spain E-28006 IC, Inst Estructura Mat, E-28006 Madrid, Spain Univ Paris 06, CNRS, URA, LPBC, Paris, France Univ Paris 06 Paris France niv Paris 06, CNRS, URA, LPBC, Paris, France
Titolo Testata:
PHOTOCHEMISTRY AND PHOTOBIOLOGY
fascicolo: 2, volume: 74, anno: 2001,
pagine: 172 - 183
SICI:
0031-8655(200108)74:2<172:IOHWSA>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
SIDE-CHAIN CONFORMATION; AROMATIC AMINO-ACIDS; PROTEIN-KINASE-C; BINDING-SITES; ANTIRETROVIRAL ACTIVITY; EXCITATION PROFILES; LASER EXCITATION; TRYPTOPHAN; SPECTRA; FLUORESCENCE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
57
Recensione:
Indirizzi per estratti:
Indirizzo: Miskovsky, P Safarik Univ, Dept Biophys, Jesenna 5, Kosice 04154, SlovakiaSafarik Univ Jesenna 5 Kosice Slovakia 04154 04154, Slovakia
Citazione:
P. Miskovsky et al., "Interaction of hypericin with serum albumins: Surface-enhanced Raman spectroscopy, resonance Raman spectroscopy and molecular modeling study", PHOTOCHEM P, 74(2), 2001, pp. 172-183

Abstract

Surface-enhanced Raman spectroscopy, resonance Raman spectroscopy and molecular modeling were employed to study the interaction of hypericin (Hyp) with human (HSA), rat (RSA) and bovine (BSA) serum albumins. The identification of the binding site of Hyp in serum albumins as well as the structural model for Hyp/HSA complex are presented. The interactions mainly reflect: (1) a change of the strength of H bonding at the N1-H site of Trp; (2) a change of the Trp side-chain conformation; (3) a change of the hydrophobicity of the Trp environment; and (4) a formation of an H-bond between the carbonyl group of Hyp and a proton donor in HSA and RSA which leads to a protonated-like carbonyl in Hyp. Our results indicate that Hyp is rigidly bound in IIA subdomain of HSA close to Trp214 (distance 5.12 Angstrom between the centers of masses). In the model presented the carbonyl group of Hyp is hydrogen bonded to Asn458. Two other candidates for hydrogen bonds have been identified between the bay-region hydroxyl group of Hyp and the carbonyl group of the Trp214 peptidic link and between the peri-region hydroxyl group of Hyp and the Asn458 carbonyl group. It is shown that the structures of the Hyp/HSA and Hyp/RSA complexes are similar to, and in some aspects different from, those found for the Hyp/BSA complex. The role of aminoacid sequence inthe IIA subdomains of HSA, RSA and BSA is discussed to explain the observed differences.

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Documento generato il 28/09/20 alle ore 04:20:00