Thermodynamics of Polypeptide Supramolecular Assembly in the Short-Chain Limit.The self-assembly of peptides into ordered supramolecular structures, such as fibrils and crystals, is of relevance in such diverse areas as molecular medicine and materials science.  However, little information is available about the fundamental thermodynamic driving forces of these types of self-assembly processes.  Here, we investigate in detail the thermodynamics of assembly of diphenylalanine (FF).  We find that the thermodynamics of FF assembly displays the typical characteristics of hydrophobic desolvation processes, and detailed analysis of the temperature dependence of the kinetics of assembly within the framework of crystallization theories reveals that the transition state from solution to crystalline aggregates is enthalpically unfavorable and entropically favorable, qualitatively similar to what has been found for longer sequences. 
THERM