How does sucrose stabilize the native state of globular proteins?

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• 作者：Giuseppe  ; Graziano  ; ;   ; ^{graziano@unisannio.it}
• 关键词：Sucrose ; Protein conformational stability ; Solvent-excluded volume effect ; Work of cavity creation
• 刊名：International Journal of Biological Macromolecules
• 出版年：2012
• 出版时间：1 January 2012
• 年：2012
• 卷：50
• 期：1
• 页码：230-235
• 全文大小：269 K

文摘

It is well known that sucrose stabilizes the native state of globular proteins against both chemical denaturants and temperature. A largely accepted explanation of sucrose-induced stabilization is not yet emerged. It is shown that the same theoretical approach able to rationalize the occurrence of cold denaturation, the contrasting role of GdmCl and Gdm₂SO₄, and the TMAO counteraction of urea denaturing activity [PCCP 12 (2010) 14245; PCCP 13 (2011) 12008; PCCP 13 (2011) 17689] works well also in the case of sucrose. The solvent-excluded volume effect plays the fundamental role because sucrose addition to water causes a marked increase in volume packing density due to the large size of sucrose molecules, that act as crowding agents.