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The interaction of left- and right-handed polylysine chains (poly(D-lysine) and poly(L-lysine)) results in a dramatic increase in the propensity to form aggregated beta-sheet structure (and amyloid-like fibrils), which is reflected by an approximately 15 degrees C decrease of temperature of the alpha-helix-to-beta-sheet transition. While a relative volume expansion of 13-19 mL x mol(-1) accompanies the alpha-to-beta-transition in a single enantiomer, this does not hold true for the mixture, which, along with substantially more negative heat capacity changes, points to a lower solvent-entropy cost of the transition as the possible thermodynamic driving force of the diastereomeric aggregation. The underlying solvational mechanism may be one of the decisive factors responsible for the spontaneous protein aggregation in vivo and, as such, may shed new light on the molecular basis of amyloid-associated diseases.
Dzwolak et al. (Mon,) studied this question.