Modulation of the hydrogen bonding structure of water by renal osmolytes

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Title
Modulation of the hydrogen bonding structure of water by renal osmolytes
Author(s)
Pramod Kumar Verma; Hochan Lee; Joon-Young Park; Joon-Hyung Lim; Michał Maj; Jun-Ho Choi; Kyung-Won Kwak; Minhaeng Cho
Publication Date
2015-07
Journal
JOURNAL OF PHYSICAL CHEMISTRY LETTERS, v.6, no.14, pp.2273 - 2279
Publisher
AMER CHEMICAL SOC
Abstract
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. © 2015 American Chemical Society
URI
https://pr.ibs.re.kr/handle/8788114/1966
ISSN
1948-7185
Appears in Collections:
Center for Molecular Spectroscopy and Dynamics(분자 분광학 및 동력학 연구단) > Journal Papers (저널논문)
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