NDLI: Preferential exclusion of sucrose from recombinant interleukin-1 receptor antagonist: role in restricted conformational mobility and compaction of native state.

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Preferential exclusion of sucrose from recombinant interleukin-1 receptor antagonist: role in restricted conformational mobility and compaction of native state.

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Preferential exclusion of sucrose from recombinant interleukin-1 receptor antagonist: role in restricted conformational mobility and compaction of native state.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Carpenter, J. F. Peterson, B. Arakawa, T. Kendrick, B. S. Chang, B. S. Randolph, T. W. Manning, M. C.
Description	Author Affiliation: Kendrick BS ( Department of Pharmaceutical Sciences, School of Pharmacy, University of Colorado Health Sciences, Denver, CO 80262, USA.);
Abstract	Understanding the mechanism for sucrose-induced protein stabilization is important in many diverse fields, ranging from biochemistry and environmental physiology to pharmaceutical science. Timasheff and Lee [Lee, J. C. & Timasheff, S. N. (1981) J. Biol. Chem. 256, 7193-7201] have established that thermodynamic stabilization of proteins by sucrose is due to preferential exclusion of the sugar from the protein's surface, which increases protein chemical potential. The current study measures the preferential exclusion of 1 M sucrose from a protein drug, recombinant interleukin 1 receptor antagonist (rhIL-1ra). It is proposed that the degree of preferential exclusion and increase in chemical potential are directly proportional to the protein surface area and that, hence, the system will favor the protein state with the smallest surface area. This mechanism explains the observed sucrose-induced restriction of rhIL-1ra conformational fluctuations, which were studied by hydrogen-deuterium exchange and cysteine reactivity measurements. Furthermore, infrared spectroscopy of rhlL-1ra suggested that a more ordered native conformation is induced by sucrose. Electron paramagnetic resonance spectroscopy demonstrated that in the presence of sucrose, spin-labeled cysteine 116 becomes more buried in the protein's interior and that the hydrodynamic diameter of the protein is reduced. The preferential exclusion of sucrose from the protein and the resulting shift in the equilibrium between protein states toward the most compact conformation account for sucrose-induced effects on rhIL-1ra.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	22
Volume Number	94
Language	English
Publisher	National Academy of Sciences
Publisher Date	1997-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Receptors, Interleukin-1 Antagonists & Inhibitors Sialoglycoproteins Chemistry Drug Effects Sucrose Pharmacology Chemical Phenomena Chemistry, Physical Circular Dichroism Cysteine Deuterium Oxide Electron Spin Resonance Spectroscopy Interleukin 1 Receptor Antagonist Protein Models, Chemical Protein Conformation Recombinant Proteins Scattering, Radiation Spectrophotometry, Infrared Spectrophotometry, Ultraviolet Surface Properties Thermodynamics Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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