INVESTIGADORES
PICO Guillermo Alfredo
artículos
Título:
Thermal features of the bovine serum albumin unfolding by polyethylene glycols
Autor/es:
FARRUGGIA, B; NERLI, BIBIANA; DI NUCI, HERNÁN; RIGATUSSO, RUBÉN; GUILLERMO ALFREDO PICO
Revista:
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
Editorial:
elsevier
Referencias:
Lugar: Amsterdant; Año: 1999 vol. 26 p. 23 - 33
ISSN:
0141-8130
Resumen:
Albumin showed very poor affinity for polyethylene glycol molecular weight (Mw) 1000 (30 M1) and Mw 8000 (400 M1)
(PEG 1000 and PEG 8000). Polyethylene glycol of low Mw favours the ionization of the tyrosine (TYR) residues of albumin. Such
variation might be a consequence of the change in dielectric constant at the domain of the protein by PEG binding. PEGs of high
Mws stabilize the native compact state of human albumin showing negative preferential interaction with the protein. Interaction
between PEGs and albumin is thermodynamically unfavourable, and becomes even more unfavourable for denatured proteins
whose surface areas are larger than those of native ones leading to a stabilization of the unfolded state, which is manifested as
a lowering of the thermal transition temperature. PEG 8000 perturbs the structure of the protein surface, partially modifying the
layer of water and the microenvironment of the superficial aromatic residues (tryptophan, TRP and TYR) which is in agreement
with the modifications of the UV spectrum of albumin by PEG 8000 and circular dichroism (CD) spectrum at high temperatures.
(PEG 1000 and PEG 8000). Polyethylene glycol of low Mw favours the ionization of the tyrosine (TYR) residues of albumin. Such
variation might be a consequence of the change in dielectric constant at the domain of the protein by PEG binding. PEGs of high
Mws stabilize the native compact state of human albumin showing negative preferential interaction with the protein. Interaction
between PEGs and albumin is thermodynamically unfavourable, and becomes even more unfavourable for denatured proteins
whose surface areas are larger than those of native ones leading to a stabilization of the unfolded state, which is manifested as
a lowering of the thermal transition temperature. PEG 8000 perturbs the structure of the protein surface, partially modifying the
layer of water and the microenvironment of the superficial aromatic residues (tryptophan, TRP and TYR) which is in agreement
with the modifications of the UV spectrum of albumin by PEG 8000 and circular dichroism (CD) spectrum at high temperatures.
1) and Mw 8000 (400 M1)
(PEG 1000 and PEG 8000). Polyethylene glycol of low Mw favours the ionization of the tyrosine (TYR) residues of albumin. Such
variation might be a consequence of the change in dielectric constant at the domain of the protein by PEG binding. PEGs of high
Mws stabilize the native compact state of human albumin showing negative preferential interaction with the protein. Interaction
between PEGs and albumin is thermodynamically unfavourable, and becomes even more unfavourable for denatured proteins
whose surface areas are larger than those of native ones leading to a stabilization of the unfolded state, which is manifested as
a lowering of the thermal transition temperature. PEG 8000 perturbs the structure of the protein surface, partially modifying the
layer of water and the microenvironment of the superficial aromatic residues (tryptophan, TRP and TYR) which is in agreement
with the modifications of the UV spectrum of albumin by PEG 8000 and circular dichroism (CD) spectrum at high temperatures.