Detection and characterization of an acid-induced folding intermediate of endostatin

Biochemical and Biophysical Research Communications
Xiaoyu WuYongzhang Luo

Abstract

Endostatin, an important angiogenesis inhibitor, is very acid resistant. We are particularly interested in knowing that whether or not endostatin can form a folding intermediate during acid titration. 1H-NMR, CD spectrum, and ANS binding assay show that endostatin at pH 2.0 contains little tertiary structure, but retains substantial secondary structure with strong ANS binding, and Na2SO4 or TFE is found to strongly stabilize endostatin at pH 2.0. All these observations are consistent with the formation of a folding intermediate at pH 2.0. Kinetics studies show that sulfate anions significantly slow down the process for endostatin to reach its equilibrium state at pH 2.0. A regular increase in the amount of alpha-helix content of the intermediate of endostatin at pH 2.0 is found when the concentration of TFE is increased in the range of 0-40%, suggesting that endostatin has an intrinsic alpha-helical propensity.

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Citations

Jul 27, 2010·International Journal of Pharmaceutics·Boyu MengXiaojin Yin
May 17, 2008·Analytical Biochemistry·Rosa Maria Chura-ChambiLigia Morganti
May 28, 2009·IUBMB Life·Yan FuYongzhang Luo
Jan 10, 2008·Archives of Biochemistry and Biophysics·Yan FuYongzhang Luo
Nov 5, 2005·The Journal of Biological Chemistry·Yingbo HeYongzhang Luo

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