Publication

Determination of drug binding sites to proteins by electrospray ionisation mass spectrometry: the interaction of cisplatin with transferrin

2002
Journal Articles

Abstract

Cisplatin, CiS-[PtCl2(NH3)(2)], is known to bind to human serum transferrin, but the binding site remains a matter of some debate. Electrospray ionisation mass spectrometry has been used to characterise the interaction of cisplatin with transferrin. The studies indicate that cisplatin initially docks with, and subsequently bonds covalently to, the hydroxyl functional group of threonine 457, with the loss of HCl affording a transferrin-O-PtCl(NH3)(2) adduct. Copyright (C) 2002 John Wiley Sons, Ltd.

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2002
Journal Articles

Abstract

Official source

Related concepts (28)

Transferrin

Transferrins are glycoproteins found in vertebrates which bind and consequently mediate the transport of iron (Fe) through blood plasma. They are produced in the liver and contain binding sites for two Fe3+ ions. Human transferrin is encoded by the TF gene and produced as a 76 kDa glycoprotein. Transferrin glycoproteins bind iron tightly, but reversibly. Although iron bound to transferrin is less than 0.1% (4 mg) of total body iron, it forms the most vital iron pool with the highest rate of turnover (25 mg/24 h).

Functional group

In organic chemistry, a functional group is a substituent or moiety in a molecule that causes the molecule's characteristic chemical reactions. The same functional group will undergo the same or similar chemical reactions regardless of the rest of the molecule's composition. This enables systematic prediction of chemical reactions and behavior of chemical compounds and the design of chemical synthesis. The reactivity of a functional group can be modified by other functional groups nearby.

Serum iron

Serum iron is a medical laboratory test that measures the amount of circulating iron that is bound to transferrin and freely circulate in the blood. Clinicians order this laboratory test when they are concerned about iron deficiency, which can cause anemia and other problems. 65% of the iron in the body is bound up in hemoglobin molecules in red blood cells. About 4% is bound up in myoglobin molecules. Around 30% of the iron in the body is stored as ferritin or hemosiderin in the spleen, the bone marrow and the liver.

Related publications (1)

Determination of drug binding sites to proteins by electrospray ionisation mass spectrometry: the interaction of cisplatin with transferrin

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Reversible Oriented Surface Immobilization of Functional Proteins on Oxide Surfaces