期刊
BIOPHYSICAL CHEMISTRY
卷 107, 期 2, 页码 175-187出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bpc.2003.09.004
关键词
bovine serum albumin; protein aggregation; infrared spectroscopy; conformational changes; static light scattering; dynamic light scattering
To investigate which type of structural and conformational changes is involved in the aggregation processes of bovine serum albumin (BSA), we have performed thermal aggregation kinetics in D2O solutions of this protein. The tertiary conformational. changes are followed by Amide II band, the secondary structural changes and the formation of beta-aggregates by the Amide I' band and, finally, the hydrodynamic radius of aggregates by dynamic light scattering. The results show, as a function of pD, that: tertiary conformational changes are more rapid as pD increases; the aggregation proceeds through formation of ordered aggregates (oligomers) at pD far from the isoelectric point of the protein; disordered structures add as the pD decreases. Moreover, beta-aggregates seem to contribute only to oligomers formation, as showed by the good correlation between kinetics of scattering intensity and IR absorption intensity. These results indicate for BSA a general mechanism of aggregation composed by partial unfolding of the tertiary structure and by the decrease of alpha-helix and random coil contents in favor of beta-sheet aggregates. This mechanism strictly depends on pD, and gives rise to almost two distinct types of macromolecular aggregates. (C) 2003 Elsevier B.V. All rights reserved.
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