Binding Interaction Between Prazosin and Immobilized Receptor by Frontal Analysis View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2012-04

AUTHORS

Xinfeng Zhao, Haiyan Lu, Jing Huang, Jianbin Zheng, Xiaohui Zheng, Youyi Zhang

ABSTRACT

Binding interaction between ligand and G-protein coupled receptor plays an important role in the several steps of exertion of therapeutic effect by a drug and has become increasingly interesting to pharmacists, chemists, biologists and companies. α1-Adrenoceptor (α1-AR) was purified from cell line which stably expressed α1-AR and evenly immobilized on the surface of macroporous silica gel to prepare a novel stationary phase for investigating the interaction between drug and receptor. Control drugs of α1-AR including phentolamine, terazosin and urapidil were used to characterize the retention properties of the stationary phase containing the receptor. Further work was performed to calculate the binding sites and association constant of prazosin binding to the immobilized receptor. The results presented a value of 4.55 × 10−7 M−1 for binding sites and of 2.2 × 104 M for the association constant during the interaction between prazosin and α1-AR. The proposed affinity method was stable at least in seven consecutive days, as well as had the primary bioactivities of recognizing and binding the ligand, providing an alternative for representing the interaction between drug and functional protein. More... »

PAGES

411-415

Identifiers

URI

http://scigraph.springernature.com/pub.10.1007/s10337-012-2198-4

DOI

http://dx.doi.org/10.1007/s10337-012-2198-4

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1005070082


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