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Titolo:
Stabilizing effects of various polyelectrolyte multilayer films on the structure of adsorbed/embedded fibrinogen molecules: An ATR-FTIR study
Autore:
Schwinte, P; Voegel, JC; Picart, C; Haikel, Y; Schaaf, P; Szalontai, B;
Indirizzi:
ULP, CNRS, Inst Charles Sadron, F-67083 Strasbourg, France ULP Strasbourg France F-67083 Charles Sadron, F-67083 Strasbourg, France Univ Strasbourg 1, INSERM, U424, Unite Format & Rech Odontol, F-67085 Strasbourg, France Univ Strasbourg 1 Strasbourg France F-67085 , F-67085 Strasbourg, France Hungarian Acad Sci, Biol Res Ctr, Inst Biophys, H-6701 Szeged, Hungary Hungarian Acad Sci Szeged Hungary H-6701 Biophys, H-6701 Szeged, Hungary
Titolo Testata:
JOURNAL OF PHYSICAL CHEMISTRY B
fascicolo: 47, volume: 105, anno: 2001,
pagine: 11906 - 11916
SICI:
1520-6106(20011129)105:47<11906:SEOVPM>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
QUANTITATIVE IR SPECTROPHOTOMETRY; TRANSFORM INFRARED-SPECTROSCOPY; WATER H2O SOLUTIONS; SECONDARY STRUCTURE; PEPTIDE COMPOUNDS; ABSORPTION-BANDS; GLUCOSE-OXIDASE; PROTEINS; ADSORPTION; POLYPEPTIDES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Physical, Chemical & Earth Sciences
Citazioni:
42
Recensione:
Indirizzi per estratti:
Indirizzo: Schaaf, P ULP, CNRS, Inst Charles Sadron, 6 Rue Boussingault, F-67083 Strasbourg, France ULP 6 Rue Boussingault Strasbourg France F-67083 sbourg, France
Citazione:
P. Schwinte et al., "Stabilizing effects of various polyelectrolyte multilayer films on the structure of adsorbed/embedded fibrinogen molecules: An ATR-FTIR study", J PHYS CH B, 105(47), 2001, pp. 11906-11916

Abstract

The structural changes in fibrinogen as a consequence of its adsorption onto the surface of or its embedding into the interior of poly (allyl ami ne hydrochloride) (PAH) or poly(styrenesulfonate) (PSS) multilayers are investigated by means of attenuated total reflection Fourier transform infrared (ATR-FTIR) spectroscopy. It is found that both adsorption and embedding preserve the secondary structure of the fibrinogen molecules. Furthermore, the interactions of the polyelectrolytes with the protein molecules prevent their aggregation, especially in the embedded state, at room temperature. Thus, it seems that the structure and the biological activity of proteins adsorbed on or embedded in polyelectrolyte multilayers could largely be preserved, which opens up great perspectives in the design of new bioactive surfaces. The nature and the extent of the polyelectrolyte-protein interactions are further studied via analysis of the thermotropic responses of the different architectures. It is found that both PAH- and PSS-terminated polyclectrolyte multilayers can elevate the onset temperature of the structural chances in adsorbed/embedded fibrinogen molecules by about 5 degreesC as comparedwith that for fibrinogen in solution. These polyelectrolytes also broaden the thermally induced structural transitions in the adsorbed/embedded fibrinogen molecules. The magnitude of these thermally induced structural changes is polyelectrolyte- and architecture-dependent. Whereas multilayer PAH-fibrinogen and multilayer PSS-fibrinogen constructions exhibit roughly the same large-scale thermally induced structural changes, in all architectures where fibrinogen is embedded the scale of these structural changes is restricted. The restriction becomes stronger as the presence of PSS at the polyelectrolyte- fibrinogen interfaces increases (PAH-fib-PAH < PAH-fib-PSS approximate to PSS-fib-PAH < PSS-fib-PSS). In the PSS-fib-PSS arrangement, the secondary structure of fibrinogen as determined from its infrared spectrum changes only slightly up to 90 degreesC. The underlying processes of the thermally induced structural changes is, in addition, different for fibrinogenmolecules adsorbed onto or embedded into PAH-terminated polyelectrolyte multilayers. A tentative model based on "encapsulation" of the embedded protein by the polyelectrolytes is proposed to explain the observed features.

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Documento generato il 04/04/20 alle ore 11:19:10