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Protein Science (2007), 16:1193-1203. Published by Cold Spring Harbor Laboratory Press. Copyright © 2007 The Protein Society
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Parathyroid hormone is a heparin/polyanion binding protein: Binding energetics and structure modification

Tim J. Kamerzell1,2, Sangeeta B. Joshi1,2, Donald McClean3, Lori Peplinskie4, Karen Toney4, Damon Papac4, Meili Li4, and C. Russell Middaugh1

1 Department of Pharmaceutical Chemistry, University of Kansas, Lawrence, Kansas 66047, USA

(RECEIVED October 13, 2006; FINAL REVISION January 17, 2007; ACCEPTED February 22, 2007)

The interaction of four representative polyanions with parathyroid hormone (PTH) residues 1–84 has been investigated utilizing a variety of spectroscopic and calorimetric techniques. Each of the polyanions employed demonstrate enthalpically driven binding to PTH (1–84) with significant affinity. The polyanions heparin, dextran sulfate, phytic acid, and sucrose octasulfate induce {alpha}-helical structure in PTH to varying extents depending on the ratio of polyanion to protein employed. Intrinsic and extrinsic fluorescence spectroscopy suggests significant protein tertiary structure alteration upon polyanion binding. Although structural modification occurred upon polyanion binding, PTH colloidal stability was increased depending on the ratio of polyanion to protein used. Nevertheless, the bioactivity of PTH in the presence of various ratios of heparin was not altered. The potential biological significance of PTH/polyanion interactions is discussed.

Keywords: heparin/polyanion binding protein; parathyroid hormone; secondary structure; tertiary structure; energetics


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