α1-Acid Glycoprotein, Human Information

Product name:α1-Acid Glycoprotein, Human
Description of α1-Acid Glycoprotein, Human:
Human α1-acid glycoprotein (AGP) is an important drug binding plasma protein which affects pharmacokinetical properties of various
therapeutic agents. For the first time, interpretation of the induced circular dichroism (ICD) spectra of drug–AGP complexes is presented yielding
valuable information on the protein binding environment. ICD spectra were obtained by novel ligands of which AGP induced optical activity have
never been reported (primaquine, mefloquine, propranolol, terazosin, carbamazepine, rhodamine B) and by re-investigation of ICD spectra of
protein-bound drugs published earlier (chlorpromazine, dipyridamole, prazosin). Spectroscopic features of the ICD and absorption bands of drugs
combined with native AGP indicated chiral non-degenerate exciton coupling between the guest chromophore and the indole ring of an adjacent
tryptophan (Trp) residue. Results of additional CD experiments performed by using recombinant AGP mutants showed no changes in the ligand
binding ability of W122A in sharp contrast with the W25A which was unable to induce extrinsic CD signal with either ligand. Thus, these findings
unequivocally prove that, likely via π–π stacking mechanism, Trp25 is essentially involved in the AGP binding of drugs studied here as well as of
related compounds.
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