Artificial chaperoning of insulin, human carbonic anhydrase and hen egg lysozyme using linear dextrin chains – a sweet route to the native state of globular proteins

Sivakama Sundari, C. ; Raman, B. ; Balasubramanian, D. (1999) Artificial chaperoning of insulin, human carbonic anhydrase and hen egg lysozyme using linear dextrin chains – a sweet route to the native state of globular proteins FEBS Letters, 443 (2). pp. 215-219. ISSN 0014-5793

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Official URL: http://linkinghub.elsevier.com/retrieve/pii/S00145...

Related URL: http://dx.doi.org/10.1016/S0014-5793(98)01720-7

Abstract

Linear dextrins (α-1,4-D-glucopyranoside chains) are known to possess amphiphilic surfaces and solubilize lipophilic compounds. We have assessed the ability of this amphiphilic surface of dextrin to inhibit the self-aggregation and assist the refolding of proteins. Addition of decameric dextrin, or dextrin-10, in the renaturation buffer improves the refolding yield of human carbonic anhydrase from its guanidinium chloride-induced denatured state. It is also seen to inhibit the self-aggregation of insulin. The ability of dextrin-10 to interact with cetyltrimethylammonium bromide and postpone its critical micellar concentration allows the use of dextrin-10 as a 'detergent stripping agent' in a novel artificial chaperoning process described earlier. The aggregation of human carbonic anhydrase and lysozyme upon refolding is prevented by cetyltrimethylammonium bromide due to the formation of a protein-detergent complex; dextrin-10 strips off the detergent from the complex and allow the proteins to fold, thus increasing the renaturation yield. Dextran-4 (the α-1,6-D-glucopyranoside chain), which does not exhibit amphiphilic properties, does not help in such artificial chaperoning.

Item Type:Article
Source:Copyright of this article belongs to Federation of European Biochemical Societies.
Keywords:Linear Dextrin; Dextran; Artificial Chaperone; Protein Refolding
ID Code:1203
Deposited On:05 Oct 2010 12:45
Last Modified:16 May 2016 12:21

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