Modulation of the hydrogen bonding structure of water by renal osmolytes

Pramod Kumar Verma, Hochan Lee, Joon Young Park, Joon Hyung Lim, Michał Maj, Jun Ho Choi, Kyung Won Kwak, Minhaeng Cho

Research output: Contribution to journalArticlepeer-review

22 Citations (Scopus)


Osmolytes are an integral part of living organism, e.g., the kidney uses sorbitol, trimethylglycine, taurine and myo-inositol to counter the deleterious effects of urea and salt. Therefore, knowing that the osmolytes' act either directly to the protein or mediated through water is of great importance. Our experimental and computational results show that protecting osmolytes, e.g., trimethylglycine and sorbitol, significantly modulate the water H-bonding network structure, although the magnitude and spatial extent of osmolyte-induced perturbation greatly vary. In contrast, urea behaves neutrally toward local water H-bonding network. Protecting osmolytes studied here show strong concentration-dependent behaviors (vibrational frequencies and lifetimes of two different infrared (IR) probes), while denaturant does not. The H-bond donor and/or acceptor (OH/NH) in a given osmolyte molecule play a critical role in defining their action. Our findings highlight the significance of the alteration of H-bonding network of water under biologically relevant environment, often encountered in real biological systems.

Original languageEnglish
Pages (from-to)2273-2279
Number of pages7
JournalJournal of Physical Chemistry Letters
Issue number14
Publication statusPublished - 2015 Jul 16


  • MD simulation
  • hydrogen bonding
  • infrared pump-probe
  • orientational relaxation
  • population relaxation
  • renal osmolyte
  • vibrational spectroscopy

ASJC Scopus subject areas

  • Materials Science(all)
  • Physical and Theoretical Chemistry


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