Design, Synthesis and biological evaluation of catecholamine vehicle for studying dopaminergic system.
Catecholamine mimetic EDTA-bis(tyramide) was synthesized and characterized by various spectroscopic techniques (NMR, Mass spectroscopy) and λem 310 nm for the excitation at 270 nm. Molecular docking studies were performed with Human Serum Albumin (HSA: PDB 1E78), showing binding pattern with amino acid residues Arg218, Arg222 and Lys444, identifies the ligand-HSA interaction for the transportation affinity of the ligand at the specific site of the target. Subsequently binding study with HSA at λex =350 nm found to be 5.847x10(4) M(-1) shows effective quenching effect. Additionally to go more insight AChE binding affinity was investigated, which shows 90% binding affinity for the 10 mM concentration. IC50 value was was found 18.60 μM for MAO-B inhibition. Finally, EDTA-bis(tyramide) labeled with (99m) Tc to investigate its in-vivo radiopharmaceutical efficiency, having 97% binding affinity with 98% radiochemical purity. In-vivo studies were carried out for (99m) Tc- EDTA-bis(tyramide) included blood kinetics showed a quick wash out from the circulation via renal route and biodistribution revealed that maximum%ID/g was found in kidney at 1h and its scintigraphy image shows 3.96% brain uptake with respect to whole body. This article is protected by copyright. All rights reserved.
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CHEMICAL GENE-Y GENE-Y GENE-Y GENE-Y CHEMICAL CHEMICAL CHEMICAL CHEMICAL CHEMICAL CHEMICAL CHEMICAL CHEMICAL CHEMICAL
catecholamine Human Serum Albumin HSA HSA MAO-B Catecholamine EDTA-bis(tyramide) amino acid Arg Arg Lys EDTA-bis(tyramide) (99m) Tc (99m) Tc- EDTA-bis(tyramide)