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Lysozyme refolding with cyclodextrins: structure-activity relationship.

A Desai¹, C Lee, L Sharma

¹Department of Chemistry, Central Michigan University, Dow 346, Mt. Pleasant, MI 48859, USA.

|June 2, 2006

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Cyclodextrins (CDs) aid protein refolding by preventing aggregation. Neutral CDs, especially alpha-cyclodextrin, are effective, while charged CDs hinder refolding, suggesting CDs act similarly to chaotropic agents.

Area of Science:

Biochemistry
Materials Science

Background:

Cyclodextrins (CDs) are known to suppress protein aggregate formation during refolding.
Understanding the mechanism of CD-assisted protein refolding is crucial for identifying effective protein folding agents.

Purpose of the Study:

To investigate the structure-activity relationship between cyclodextrin chemistry and protein refolding.
To compare the refolding of lysozyme and carbonic anhydrase with various CDs.

Main Methods:

Performed a structure-activity relationship study of cyclodextrins (CDs) and protein refolding.
Compared the effects of natural and modified CDs on lysozyme and carbonic anhydrase refolding.
Utilized electrophoresis to analyze aggregation stages.

Main Results:

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Neutral CDs, particularly alpha-cyclodextrin, were more effective than charged CDs in promoting lysozyme refolding.
Anionic substituents on CDs promoted aggregation and abolished refolding ability, an effect more pronounced in lysozyme.
CDs that promoted refolding arrested aggregation at the soluble aggregate stage.

Conclusions:

The anti-aggregation properties of CDs are key to their protein refolding ability.
CDs may function similarly to chaotropic agents in protein refolding.
Neutral CDs are promising candidates for protein folding agents.