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Background:  Mycobacterial α-crystallin (Acr) is a chaperone that prevents misfolding of proteins when  Mycobacterium tuberculosis  is found in a latent form in the host tissue.    Methods:  Using insulin as a model substrate and utilizing polynomial graphs, we attempted to predict molecular-level interactions that are a function of the oligomeric state of the recombinant protein. The chaperone activity of the recombinant oligomeric Acr was measured at 60°C with Acr samples obtained before gel filtration chromatography and compared with a gel-filtered sample.    Results:  The polynomial graphs constructed showed improved molecular coverage of the insulin B chain by the oligomer. The 2  nd  order coefficient is the one that changes with the oligomeric ratio of Acr and improves chaperone activity. Polynomial analysis suggested that it could be a useful parameter to predict chaperone activity for potential  in vitro  batches of  M. tuberculosis  Acr based on the dynamic nature of the association and disassociation of oligomers.    Conclusions : The results showed that coverage of insulin B chain improved with higher ratio of 9-mer as compared to lower ratios. This was shown by both simulation plots and actual assay data. The polynomial graphs showed increase in the 2  nd  order coefficient, thus suggesting the important role of oligomerisation in improved molecular coverage of insulin B chain.

Prediction of recombinant Mycobacterium tuberculosis α-crystallin oligomer chaperone activity using polynomial graphs