Hydration Dynamics of Water near an Amphiphilic Model Peptide at Low Hydration Levels: A Dielectric Relaxation Study

Abstract

A dielectric relaxation study of aqueous solutions of the amphiphilic model peptide N-acetyl-leucine amide (NALA) at 298 K over a wide range of hydration levels is presented. The experiments range from states where water builds up several hydration layers to states where single water molecules or small water clusters are shared by several NALA molecules. The dielectric spectra reveal two modes on the 10 and 100 ps timescales. These are largely broadened with regard to the Lorentzian shape caused by simple Debye-type relaxation, and are well described by the Kohlrausch-Williams-Watts stretched exponential function. The fast mode is assigned to water reorientation comprising bulk water as well as hydration water. Even when all water molecules are in contact with the solute, this fast component is dominant, and its mean relaxation time is retarded by less than a factor of two relative to neat water. The amplitude of the slow process is far higher than expected for the dipolar reorientation of the solute. The observations are consistent with results from molecular dynamics simulations for a similar model peptide reported in the literature. They suggest that the slow relaxation mode is mainly founded in peptide-water dipolar couplings, with some additional contribution from slowly reorienting hydration water molecules. The results are discussed with regard to the hydration dynamics of proteins and the interpretation of dielectric spectra of protein solutions.

Interfacial water at the trialanine hydrophilic surface: a DFT electronic structure and bottom-up investigation

“…[5][6][7][8][9][10][11][12]21 The formation of strong H-bonds, which disrupts the water structure and avoids synergistic water molecule reorientation in the immediate vicinity of the peptide, is responsible for the slowdown of water motion. [5][6][7][8][9][10][11][12]21 The formation of strong H-bonds, which disrupts the water structure and avoids synergistic water molecule reorientation in the immediate vicinity of the peptide, is responsible for the slowdown of water motion.…”

Quantum Mechanics Approach to Hydration Energies and Structures of Alanine and Dialanine

“…[9][10][11][12] From the experimental point of view,t here is no exhaustive experimental technique that directly probess pecific biomolecule-water interactions in solution, sincec hanges in geometricala rrangement are too fast, on the picosecondt imescale. [13] Nevertheless, neutron scattering, [14] NMR, [15,16] terahertz, [17][18][19] dielectric relaxation, [20] and fluorescence [21] spectroscopy has shownt hat molecular reorientation occurs more slowly than in bulk water,m ainly because of the peptide-water H-bonds and the topologically het-erogeneous nature of ap eptide surface, which disrupts the synergistic water-water reorientation mechanisms.…”

Broadband dielectric spectroscopy on human blood

“…Finally, a dispersion with low dipolar strength located in the frequency regime between the β-and γ-dispersion was identified by Schwan [12]. The origin of the δ-dispersion and the possible role of bound water in its generation is controversially discussed [30,31,32,33,34,35,36,37,38].…”