Water Dynamics in Highly Concentrated Protein Systems -- Insight from Nuclear Magnetic Resonance Relaxometry

TL;DR

This study investigates water dynamics in highly concentrated BSA protein solutions using NMR relaxometry across various frequencies and temperatures, revealing surface diffusion mediated by adsorption as the most plausible mechanism.

Contribution

It introduces a comprehensive analysis of water motion in concentrated protein systems using multiple relaxation models, identifying surface diffusion mediated by adsorption as the key process.

Findings

Surface diffusion mediated by adsorption best explains water dynamics.

Quantitative parameters of water motion were determined.

Water relaxation behavior varies with protein concentration and temperature.

Abstract

1H spin-lattice relaxation experiments have been performed for water - Bovine Serum Al-bumin (BSA) mixtures including 20% wt and 40% wt of BSA. The experiments have been carried out in a frequency range encompassing three orders of magnitude, from 10 kHz to 10 MHz, versus temperature. The relaxation data have been thoroughly analyzed in terms of several relaxation models with the purpose to reveal the mechanisms of water motion. For this purpose four relaxation models have been used: the data have been decomposed into relaxation contributions expressed in terms of Lorentzian spectral densities, then three dimensional translation diffusion has been assumed, next two dimensional surface diffusion has been considered and eventually, a model of surface diffusion mediated by acts of adsorption to the surface has been employed. In this way it has been demonstrated that the last concept is most plausible. Parameters describing the dynamics in a quantita-tive manner have been determined and discussed.