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Protein aggregation is believed to occur through the formation of misfolded conformations. It is expected\udthat, in order to minimize aggregation, an effective small molecule chaperone would destabilize these\udintermediates. To study the mechanism of a chemical chaperone, we have designed a series of mutant\udproteins in which a tryptophan residue experiences different local environments and solvent exposures. We\udshow that these mutants correspond to a series of conformationally altered proteins with varying degree of\udmisfolding stress and aggregation propensities. Using arginine as a model small molecule, we show that a\udcombination of unfolded state contraction and denaturant like properties results in selective targeting and\uddestabilization of the partially folded proteins. In comparison, the effect of arginine towards the folded like\udcontrol mutant, which is not aggregation prone, is significantly less. Other small molecules, lacking either of\udthe above two properties, do not offer any specificity towards the misfolded proteins

A small molecule chemical chaperone optimizes its unfolded state contraction and denaturant like properties