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Type: Artigo de periódico
Title: Calorimetric and structural investigation of the interaction of lysozyme and bovine serum albumin with poly(ethylene oxide) and its copolymers
Author: Almeida, NL
Oliveira, CLP
Torriani, IL
Loh, W
Abstract: This work reports investigations aiming at verifying the occurrence of specific interactions between lysozyme or bovine serum albumin (BSA) and poly(ethylene oxide) and its copolymers with poly(propylene oxide). Thermal stability of these proteins, followed by means of high sensitivity DSC, was found to be mostly unaffected by the presence of these polymers. Chromatographic experiments (reverse-phase HPLC and size exclusion chromatrography) did not reveal any sign of specific interaction for these mixtures, either. Isothermal titration calorimetry revealed an increase in enthalpy for the mixtures, represented by a positive enthalpy of transfer for these proteins from buffer to polymer solutions. Moreover, SAXS analyses confirmed that at ambient temperatures these polymers do not affect lysozyme structure. In summary, no evidence is found to support earlier suggestions that some kind of complex could be formed between these proteins and poly(ethylene oxide) or its copolymers, but the present results suggest the occurrence of entropically driven hydrophobic effects. (C) 2004 Elsevier B.V. All rights reserved.
Subject: protein denaturation
bovine serum albumin
poly(ethylene oxide)
Country: Holanda
Editor: Elsevier Science Bv
Citation: Colloids And Surfaces B-biointerfaces. Elsevier Science Bv, v. 38, n. 41671, n. 67, n. 76, 2004.
Rights: fechado
Identifier DOI: 10.1016/j.colsurfb.2004.08.004
Date Issue: 2004
Appears in Collections:Unicamp - Artigos e Outros Documentos

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