Interaction of recombinant human epidermal growth factor with phospholipid vesicles. A steady-state and time-resolved fluorescence study of the bis-tryptophan sequence (TRP49-TRP50)

1992 ◽  
Vol 21 (5) ◽  
pp. 337-344 ◽  
Author(s):  
Ines M. Li De La Sierra ◽  
Michel Vincent ◽  
Gabriel Padron ◽  
Jacques Gallay
Keyword(s):  
Steady State ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Phospholipid Vesicles ◽  
Time Resolved Fluorescence ◽  
Fluorescence Study ◽  
Time Resolved ◽  
Human Epidermal Growth Factor ◽  
Epidermal Growth

An ultrasensitive time-resolved immunofluorometric assay of human epidermal growth factor

1986 ◽  
Vol 157 (2) ◽  
pp. 208-211 ◽  
Author(s):  
K. Pesonen ◽  
H. Alfthan ◽  
U.-H. Stenman ◽  
L. Viinikka ◽  
J. Perheentupa
Keyword(s):  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Time Resolved ◽  
Human Epidermal Growth Factor ◽  
Epidermal Growth

Rapid Screening for EGFR Inhibitor in Rhei Radix et Rhizoma by HTRF Assay Coupled with HPLC Peak Fractionation

Planta Medica ◽  
2020 ◽  
Author(s):  
Yu Fu ◽  
Zhishen Xie ◽  
Peng Zhao ◽  
Shuangshuang Lv ◽  
Suiqing Chen
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Screening Method ◽  
Growth Factor Receptor ◽  
Rapid Screening ◽  
Time Resolved Fluorescence ◽  
Time Resolved ◽  
Hplc Peak ◽  
Epidermal Growth

AbstractIn this paper, an HPLC peak fractionation approach combined with homogeneous time-resolved fluorescence analysis is proposed for screening epidermal growth factor receptor inhibitors from Rhei Radix et Rhizoma. With this approach, the amount of sample used for a single HPLC run is sufficient for performing a multiple assay due to the miniaturization ability of the homogeneous time-resolved fluorescence technology. This allows for improving the stability and repeatability of the activity assay for each fraction. From a total of 26 fractions collected from the Rhei Radix et Rhizoma extract, 13 fractions exhibit inhibitory activity against the epidermal growth factor receptor. The structures of activity compounds were determined by HPLC-LTQ-Orbitrap MS, revealing the presence of gallic acid, rhein, and emodin with IC50 values of 21.5, 5.29, and 10.2 µM, respectively. The ligand epidermal growth factor receptor interactions were explored by molecular docking simulations, and the inhibitory effects of the three compounds on A549 cell growth were tested in vitro by an MTT assay. This study demonstrates the suitability of the present screening method for drug discovery in natural products.

Sign in / Sign up

Export Citation Format

Share Document