AI Article Synopsis
- The study explores how alpha-cyclodextrin (alpha-CyD) acts as a chaperone by creating a microenvironment around alcohol dehydrogenase (ADH), which helps prevent its aggregation.
- Experimental results showed that the interaction between alpha-CyD and ADH leads to a reduction in the quantity and size of polymerized molecules.
- Computational analyses confirmed that alpha-CyD effectively binds to a specific region on ADH, facilitating a protective environment that improves solubility and hinders enzyme polymerization.
Article Abstract
The chaperone action of alpha-cyclodextrin (alpha-CyD), based on providing beneficial microenvironment of hydrophobic nanocavity to form molecular complex with alcohol dehydrogenase (ADH) was examined by experimental and computational techniques. The results of UV-vis and dynamic light scattering (DLS) indicated that the chaperone-like activity of alpha-CyD depends on molecular complex formation between alpha-CyD and ADH, which caused to decrease the amount and size of polymerized molecules. Computational calculations of molecular dynamic (MD) simulations and blind docking (BD) demonstrated that alpha-CyD acts as an artificial chaperone because of its high affinity to the region of ADH's two chains interface. The hydrophobic nanocavity of alpha-CyD has the ability to form inclusion complex due to the presence of phenyl ring of aromatic phenylalanine (Phe) residue in the dimeric intersection area. Delocalization of ADH subunits, which causes the exposure of Phe110, takes part in the enzyme polymerization and has proven to be beneficial for aggregation inhibition and solubility enhancement within the host alpha-CyD-nanocavity.
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| http://dx.doi.org/10.1016/j.carres.2009.11.008 | DOI Listing |
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