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Title

THE INVESTIGATION OF COPPER-BINDING TO HUMAN SERUM ALBUMIN BY SPECTROSCOPIC METHOD

Pages

 Start Page | End Page

Keywords

COPPER (III) CHLORIDE 

Abstract

 INTRODUCTION: UNDERSTANDING THE INTERACTION BETWEEN COPPER ION AND HUMAN SERUM ALBUMIN (HSA) IS OF MAJOR PHARMACEUTICAL AND CLINICAL IMPORTANCE. HUMAN SERUM ALBUMIN (HSA) IS A SINGLE, NON-GLYCOSYLATED POLYPEPTIDE THAT ORGANIZES TO FORM A HEART-SHAPED PROTEIN WITH APPROX 67% A -HELIX BUT NO B -SHEET. IT IS RESPONSIBLE FOR THE MAINTENANCE OF BLOODP H, THE DRUG DISPOSITION AND EFFICACY, AND THE CONTRIBUTION OF COLLOIDAL OSMOTIC BLOOD PRESSURE [1-4]. THE CU2+TRANSPORT SITE OF SERUM ALBUMIN IS ONE OF THE MOST EXTENSIVELY STUDIED BINDING SITE OF ANY PROTEIN [5]. THE OBJECTIVE OF THIS STUDY WAS TO ACCESS THE CONFORMATIONAL CHANGES OF HSA DUE TO ITS BINDING TO CU2+ION BY UV-VISIBLE ABSORBANCE AND FLUORESCENCE SPECTROSCOPY.

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