NON-DETERGENT SULFOBETAINES - A NEW CLASS OF MOLECULES THAT FACILITATE IN-VITRO PROTEIN RENATURATION

Background: Attempts to renature proteins often yield aggregates rathe r than native protein, To minimize aggregation, low protein concentrat ions and/or solubilizing agents are used. Here, we test new solubilizi ng molecules, non-detergent sulphobetaines, to improve the renaturatio n of two very different enzymes, hen egg white lysozyme and bacterial beta-D-galactosidase. Results: The renaturation was conducted in the p resence of five different sulphobetaines and the yield of active enzym e was measured. The five sulphobetaines improved the yield of native l ysozyme up to 12-fold. Some sulphobetaines improved the yield of galac tosidase up to 80-fold, but one reduced it 100-fold. Conclusions: Non- detergent sulphobetaines strongly affect the balance between aggregati on and folding, Their effect depends on their structure and on their i nteractions with folding intermediates. These results should serve as a basis for designing more efficient sulphobetaines; for designing imp roved renaturation protocols using existing sulphobetaines; and for ch aracterizing folding intermediates that interact with sulphobetaines. (C) Current Biology Ltd