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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
Author(s) -
Sivakama Sundari C,
Raman B,
Balasubramanian D
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01720-7
Subject(s) - dextrin , chemistry , amphiphile , lysozyme , globular protein , liposome , biochemistry , carbonic anhydrase , organic chemistry , enzyme , starch , polymer , copolymer
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.