Chem. J. Chinese Universities

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Amino Acid Structural Descriptions Based on Random Sampling of Pseudo Atomic Probe and Its QSAR Study

ZHOU Yuan1,3,4, MEI Hu2,3, YANG Li3, ZHOU Peng2, YANG Shan-Bin3,4, LI Zhi-Liang2,3,4*   

    1. Department of Chemistry and Chemical Engineering, Hunan Engineering Institute, Xiangtan 411101, China;
    2. College of Chemistry and Chemical Engineering,
    3. College of Biological Engineering, Chongqing University, Chongqing 400044, China;
    4. State Key Laboratory of Chemo-Biosensing and Chemometrics, Hunan University, Changsha 410012, China
  • Received:2006-07-11 Revised:1900-01-01 Online:2007-07-10 Published:2007-07-10
  • Contact: LI Zhi-Liang

Abstract:

Considering the three types of non-bonding interactions between drug molecules and protein receptor molecules and using Monte Carlo's randomly sampling technology with eight pseudo atomic probes, a novel set amino acid descriptors for amino acid side chain surface electrostatic, steric and hydrophobic interaction potential field were developed successfully. By using these parameters, the QSAR study was performed for bitter tasting dipeptides(BT) and bradykinin potentiating pentapeptides(BPP) analogues, with R2 and QLOOCV2 being 0.8457, 0.851, 0.7688 and 0.7952, respectively. The effects of the type of amino acid side chain and its position in sequence of peptide were analyzed, and the results show that the ASSPF could describe the structure of peptide analogues, and an unambiguous meaning and high correlation for their activity.

Key words: Pseudo atomic probe, Random sampling on molecular surface, Amino acid side chain surface potential field descriptors, Bitter tasting dipeptide(BT), Bradykinin potentiaing pentapeptide(BPP), Quantitative structure-activity relationship(QSAR)

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