Anomalous dynamics of water at the octopeptide lanreotide surface

This work reports the study of water dynamics close to the cyclic octapeptide lanreotide from atomistic simulations of hydrated lanreotide, a cyclic octapeptide. Calculation of the hydrogen bonds between water molecules allows mapping of the hydrophilic regions of lanreotide. Whereas a super-diffusivity of the interfacial water molecules is established, a slowdown in rotational dynamics is observed, involving a decoupling between both processes. Acceleration in translation dynamics is connected to the hopping process between hydrophilic zones. Microscopically, this is correlated with the weakness of the interfacial hydrogen bonding network due to a hydrophobic interface at the origin of the interfacial sliding of water molecules. Heterogeneous rotational dynamics of water molecules close the lanreotide surface is evidenced and connected to heterogeneous hydration.

Molecular dynamics simulations of a hydrated mutated lanreotide, a cyclic octapeptide, were carried out to characterize its hydration state. We studied the water dynamics close to the peptide using atomistic simulations.