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My research interests are in the general area of iron biochemistry and are part of a major international effort to understand the role of iron in health and disease.

Iron is an element where you “Can’t live without it but you can’t live with too much of it”. It is an essential element for most forms of life but at the same time presents a danger to the cell if it is not tightly regulated. To reduce the threat posed by iron, living organisms sequester iron with transferrin, a plasma transport protein which carries iron in the circulation from the gut to the bone marrow and other tissues for the synthesis of hemoglobin and other iron containing proteins. The iron loaded transferrin delivers its content of iron by endocytosis after interaction with its receptor on the cell membrane. Once inside the cell, iron is released and stored in ferritin, the major iron storage protein in the human body. By binding iron tightly, transferrin helps to avoid the formation of free radicals reactions catalyzed by iron. These reactions are implicated in the formation of various cancers, arteriosclerosis, arthritis, and liver and heart diseases. Transferrin is also the target of chelation therapy used to treat individuals with diseases of iron overload such as “Thalassemia” and “Hemochromatosis”, the most common genetic disorder in this country, affecting 1 out of 200 individuals. The uptake and release of iron by transferrin and ferritin is a key cellular process occurring during the normal course of iron metabolism. These proteins are important for the human health as body levels and forms of iron must be appropriately maintained.

The following research projects are being currently studied:
1- The thermodynamic investigation of recombinant human serum transferrin binding to the soluble portion of the transferrin receptor.

2- The iron binding, oxidation and deposition properties in a number of ferritin samples including recombinant homopolymer human H-, L-, and heteropolymer H/L ferritin and heme-free E. coli bacterial ferritin, (EcFtnA).

3- Characterization of several L-chain ferritin mutants that cause Neuroferritinopathy (also called hereditary ferritinopathies), a severe and rare disease characterized by iron accumulation in the basal ganglia and ferritin inclusion bodies in the glia and neurons of central nervous systems and other organs.

4- Investigation of iron release from ferritin by tridentate chelate ligands of 2,6-bis[hydroxy(methyl)amino]-1,3,5-trazine family (BHT).

5- Study of the therrmodynamic stability of heteroleptic versus homoleptic metal complexes and the factors influencing the selective formation of these metal complexes.

6- Thermodynamic interaction of a novel leucine rich surface protein of Bacillus cereus protein with ferritin, heme and hemoglobin.

7- Characterization of the metal binding properties of the iron transport protein (EfeO) from Escherichia coli .

Our research is contributing to the understanding of important structure-function relationships in these crucial iron transport and storage proteins and is generating new knowledge that is essential for the rational development of new treatments for iron overload diseases and other defects in iron metabolism.

Interested students should contact Dr. Bou-Abdallah at bouabdf@postam.edu

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Opportunity for Research Dr. Fadi Bou-Abdallah Chemistry Department, Stowell Hall 302 B Ph: 315-267-2268 – Email: bouabdf@potsdam.edu
My research interests are in the general area of iron biochemistry and are part of a major international effort to understand the role of iron in health and disease. Iron is an element where you “Can’t live without it but you can’t live with too much of it”. It is an essential element for most forms of life but at the same time presents a danger to the cell if it is not tightly regulated. To reduce the threat posed by iron, living organisms sequester iron with transferrin, a plasma transport protein which carries iron in the circulation from the gut to the bone marrow and other tissues for the synthesis of hemoglobin and other iron containing proteins. The iron loaded transferrin delivers its content of iron by endocytosis after interaction with its receptor on the cell membrane. Once inside the cell, iron is released and stored in ferritin, the major iron storage protein in the human body. By binding iron tightly, transferrin helps to avoid the formation of free radicals reactions catalyzed by iron. These reactions are implicated in the formation of various cancers, arteriosclerosis, arthritis, and liver and heart diseases. Transferrin is also the target of chelation therapy used to treat individuals with diseases of iron overload such as “Thalassemia” and “Hemochromatosis”, the most common genetic disorder in this country, affecting 1 out of 200 individuals. The uptake and release of iron by transferrin and ferritin is a key cellular process occurring during the normal course of iron metabolism. These proteins are important for the human health as body levels and forms of iron must be appropriately maintained. The following research projects are being currently studied: 1- The thermodynamic investigation of recombinant human serum transferrin binding to the soluble portion of the transferrin receptor. 2- The iron binding, oxidation and deposition properties in a number of ferritin samples including recombinant homopolymer human H-, L-, and heteropolymer H/L ferritin and heme-free E. coli bacterial ferritin, (EcFtnA). 3- Characterization of several L-chain ferritin mutants that cause Neuroferritinopathy (also called hereditary ferritinopathies), a severe and rare disease characterized by iron accumulation in the basal ganglia and ferritin inclusion bodies in the glia and neurons of central nervous systems and other organs. 4- Investigation of iron release from ferritin by tridentate chelate ligands of 2,6-bis[hydroxy(methyl)amino]-1,3,5-trazine family (BHT). 5- Study of the therrmodynamic stability of heteroleptic versus homoleptic metal complexes and the factors influencing the selective formation of these metal complexes. 6- Thermodynamic interaction of a novel leucine rich surface protein of Bacillus cereus protein with ferritin, heme and hemoglobin. 7- Characterization of the metal binding properties of the iron transport protein (EfeO) from Escherichia coli . Our research is contributing to the understanding of important structure-function relationships in these crucial iron transport and storage proteins and is generating new knowledge that is essential for the rational development of new treatments for iron overload diseases and other defects in iron metabolism. Interested students should contact Dr. Bou-Abdallah at bouabdf@postam.edu