[Binding activity of polypeptide containing human Na+, K+-ATPase alpha1 subunit M1-M2 extracellular segment]
Ming-juan Zhang1, Jun Yang, Can-zhan Zhu
1Department of Cardiology, Second Affiliated Hospital, Xi'an Jiaotong University College of Medicine, Xi'an 710004, China. zhangmingjuanyj@yahoo.com
Objective:
To assess the binding activity of polypeptide containing human Na+, K+-ATPase alpha1 subunit M1-M2 extracellular segment (HES1 derivative).
Methods:
HES1 derivative was synthesized by Fmoc method and purified by high-performance liquid chromatography-mass spectrometry, and its binding activity was identified by radioligand binding assay.
Results:
3H-ouabain and synthetic HES1 derivative showed some binding activity with the equilibrium dissociation constant (KD) of 24.58 nmol/L, with the the receptor density of 492.43 fmol x mg(-1) pro. and IC50 of 3.078 x 10(-7) mol/L.
Conclusion:
HES1 derivative can bind to ouabain and has the potential of becoming an effective therapeutic agent.
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