Binding activity of polypeptide containing human Na+, K+-ATPase alpha1 subunit M1-M2 extracellular segment.
- Author:
Ming-juan ZHANG
1
;
Jun YANG
;
Can-zhan ZHU
;
Zong-ming DUAN
;
Xiao-lin NIU
;
Rong WANG
Author Information
- Publication Type:Journal Article
- MeSH: Binding Sites; drug effects; Extracellular Space; metabolism; Humans; Ouabain; chemistry; pharmacology; Peptides; chemistry; Protein Binding; Sodium-Potassium-Exchanging ATPase; chemistry; genetics; metabolism
- From: Journal of Southern Medical University 2009;29(1):13-19
- CountryChina
- Language:Chinese
-
Abstract:
OBJECTIVETo assess the binding activity of polypeptide containing human Na+, K+-ATPase alpha1 subunit M1-M2 extracellular segment (HES1 derivative).
METHODSHES1 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.
RESULTS3H-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.
CONCLUSIONHES1 derivative can bind to ouabain and has the potential of becoming an effective therapeutic agent.
