Determination and Forecast of Secondary Structure of Uremic Toxic Polypeptide

Abstract

Abstract: A uremic toxic compound with molecular weight 1007.94 was determined to be an octapeptide by mass spectrometry.Its amino-acid sequence was given as follos: Val-Val-Arg-Gly-Cys-Thr-Trp-Trp.Spin systems for amino acid residues in the octapeptide were identified through analysis of 2D NMR ¹H-¹H DQF-COSY,TOCSY and ROESY spectra acquired in H₂O and D₂O.Moreover,the complete assignment of proton resonances for the backbone and side chain was achieved.Based on the secondary chemical shift(Δδ) of the residues,the secondary structure of octapeptide was surveyed.Conformational analyses according to Chemical Shift Index(CSI) showed that the secondary structure of the octapeptide was principally α-helix.The CD spectra of the peptide in aqueous solution gave the same result.Additions of linear polymers made the conformations of octapeptide stretch.These experimental results provide a basis for further comprehension of interaction regulation between biomacromolecule and polymer absorbing materials.

Key words: Uremic toxic polypeptide, Secondary chemical shift, Lina polymer

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LI Guo-Hua, LI Ji-Hong, YANG Mei, WANG Wei, SUN Ping-Chuan, YUAN Zhi . Determination and Forecast of Secondary Structure of Uremic Toxic Polypeptide[J]. Chem. J. Chinese Universities, 2005, 26(10): 1855.

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Determination and Forecast of Secondary Structure of Uremic Toxic Polypeptide

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