Abstract
Brillouin light scattering studies of the behavior of hypersound velocity in solutions of short peptides Asp-Ser, Glu-Asp-Arg, Ala-Glu-Asp-Leu with widely varying concentrations at temperatures ranging from 295 to 360K are presented. As shown by analysis of experimental data and molecular simulation, the dipeptide Asp-Ser is characterized by formation of dimers which decompose at high temperatures. High-concentration solutions of tri- and tetrapeptides form aggregates at high temperatures which are preserved on cooling.
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