IFISE   05411
INSTITUTO DE FISIOLOGIA EXPERIMENTAL
Unidad Ejecutora - UE
artículos
Título:
Polyethyleneglycolpepsin interaction and its relationship with protein
Autor/es:
SPELZINI, D.; PELLETEIRO SALGADO, J.; PICÓ, G.; FARRUGGIA, B
Revista:
Colloids and Surfaces B: Biointerfaces
Editorial:
Elsevier
Referencias:
Lugar: Amsterdan; Año: 2008 vol. 67 p. 151 - 156
Resumen:
The interaction between the acidic protein, pepsin, and the non-charged polyethyleneglycol polymerwas
studied by dynamic light scattering, fluorescence spectroscopy and measurements of the protein thermal
stability at neutral pH. Polyethyleneglycol of average molecular mass 1450 showed a higher interaction
capacity with the protein than polyethyleneglycol of average molecular mass 8000. Polyethyleneglycol
of average molecular mass 1450 showed a molecular mechanism where the interpolymer interaction
led to the complex formation. This fact can be explained taking into account that the extended form on
this polymer molecule favours the interaction with the protein, which is highly dependent of the polymer
total concentration. Polyethyleneglycol of average molecular mass 8000 showed a cooperative interaction
between the polymer and protein molecules which was independent of the PEG concentration.