Abstract：
:Naturally occurring polyamines are known to interact with a variety of biomolecules and critically involve in some important physiological processes. They have also been shown to influence protein aggregation in vitro in some cases. The aim of the present study was to investigate how polyamines may influence the structure and thermal stability of alpha-chymotrypsin and modulate alcohol-induced aggregation of this protein. Various techniques, including turbidity measurements, tensiometry, DSC, intrinsic fluorescence and far- and near-UV circular dichroism spectroscopy were used to examine the effect of putrescine and spermidine on alpha-chymotrypsin. While slight changes in the secondary and tertiary structure of the protein was observed, a clear stabilizing effect against its thermal unfolding was achieved. Moreover, the polyamines were found to inhibit TFE-induced aggregation at 32% TFE and promote formation of non-native alpha-helices in the protein structure. Based on the observed increase in surface tension induced by polyamines, it is suggested that their effects on enhancing thermal stability and alcohol-induced alpha-helices formation may be due to their kosmotropic properties.
journal_name
Int J Biol Macromoljournal_title
International journal of biological macromoleculesauthors
Rezaei-Ghaleh N,Ebrahim-Habibi A,Moosavi-Movahedi AA,Nemat-Gorgani Mdoi
10.1016/j.ijbiomac.2007.07.018subject
Has Abstractpub_date
2007-12-01 00:00:00pages
597-604issue
5eissn
0141-8130issn
1879-0003pii
S0141-8130(07)00188-2journal_volume
41pub_type
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