FOOD SCIENCE ›› 2013, Vol. 34 ›› Issue (9): 170-174.doi: 10.7506/spkx1002-6630-201309035

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Structural Characterization and Structure-activity Relationship of ACE Inhibitory Peptides from Peanut

WANG Qiang1,WANG Chun-yan1,2,HU Hui1,LIU Hong-zhi1,LIU Li1   

  1. 1. Key Laboratory of Agro-products Processing, Ministry of Agriculture, Institute of Agro-products Processing Science and
    Technology, Chinese Academy of Agricultural Sciences, Beijing 100193, China;
    2. College of Food Science, Shenyang Agricultural University, Shenyang 110866, China
  • Received:2013-03-12 Revised:2013-04-16 Online:2013-05-15 Published:2013-05-07
  • Contact: Qiang Wang E-mail:wangqiang365@263.net

Abstract:

Peanut short-chain peptides were prepared by hydrolyzing peanut protein isolate with both alcalase and protease
N120P and separated by gel filtration chromatography and preparatve RP-HPLC. As a result, 27 components were obtained,
and P8 was found to have the highest ACE inhibitory activiy among them, with an inhbitory rate of 85.77% at 0.010 mg/mL
and an IC50 of 0.0052 mg/mL (6.42 μmol/L). The relativel molecular mass of the component P8 was 808.80 with an amino
acid sequence of Lys-Leu-Tyr-Met-Arg-Pro(KLYMRP) as determined by MALDI-TOF-TOF MS. The short-chain peptide
KLYMRP prepared with P8 by solid-phase synthesis was confirmed to have potent ACE inhibitory activity with an IC50 of
0.0038 mg/mL (4.69 μmol/L). Analysis of structure-activity relationship indicated that the short-chain peptide Lys-Leu-Tyr-
Met-Arg-Pro consisted of Pro at the C terminus and Lys at the N terminus and had strong hydrophobicity, thus facilitating
active site docking with ACE. In addition, KLYMRP formed five hydrogen bonds and one Pi-Cation interaction with residual
groups at the ACE active positions and formed coordination bonds with Zn ions. All these contributed greatly to stabilize the
conformation of the ACE-KLYMRP complex and therefore benefited ACE inhibition.

Key words: peanut peptides, amino acid sequence, ACE inhibitory activity, molecular conformation, structure-activity relationship

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