The diastereomeric assembly of polylysine is the low-volume pathway for preferential formation of β-sheet aggregates

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