Journal of Capital Medical University ›› 2016, Vol. 37 ›› Issue (6): 736-739.doi: 10.3969/j.issn.1006-7795.2016.06.004

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Detection of the interaction between the peptide and β1-adrenergic receptor autoantibodies using surface plasmon resonance

Dong Yu, Lyu Tingting, Xu Wenli, Bai Yan, Wu Ye, Liu Huirong, Wang Wen   

  1. Department of Physiology and Pathophysiology, School of Basic Medical Sciences, Capital Medical University, Beijing Key Laboratory of Metabolic Disorders Related Cardiovascular Diseases, Capital Medical University, Beijing 100069, China
  • Received:2016-10-03 Online:2016-12-21 Published:2016-12-16
  • Supported by:
    This study was supported by 973 Special Preliminary Study Plan(2014CB560704), Natural Science Foundation of Beijing(7151001).

Abstract: Objective To investigate the interaction between the peptide which mimic the structure of the second extracellular loop of the β1-adrenergic receptor (β1-AR-EC) and β1-adrenergic receptor autoantibodies (β1-AA). Methods Peptide was synthesized according to the amino acid sequence of human β1-AR-EC; a hybridoma fusion method was used to obtain anti-β1-AR-EC monoclonal antibody; the interaction between the peptide and β1-AA was detected by surface plasmon resonance (SPR); and the beating frequency experiment of neonatal rat cardiomyocytes was explored to test the neutralization of the peptide to β1-AA. Results β1-AA enhanced the beating frequency of neonatal rat cardiomyocytes (P<0.05), indicating that the β1-AA we obtained has biological activity; SPR results showed that there was a moderate binding affinity (KD) of 4.44 μmol/L between the synthetic peptide and β1-AA. Conclusion There was interaction between the synthesized peptide and β1-adrenergic receptor autoantibodies.

Key words: β1-adrenergic receptor autoantibodies(β1-AA), 26 peptide, surface plasmon resonance

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