Water proton relaxation in solutions of serum albumin from healthy donors and patients with liver and renal failures

These studies demonstrate possible connection between a decreased affinity of human serum albumin (HSA) in patients with liver and renal failures and changes of the HSA hydration state. The relaxation times, T-1 and T-2, of water protons in aqueous protein solution depend on the interaction of water molecules with biopolymer macromolecules. We compared these relaxation rimes for aqueous solutions of HSA from healthy and sick donors. For latter the amount and correlation time of the bound water are higher than those in healthy donors HSA solutions. The influence of long-chain fatty acids on the albumin hydration was found to be small.