Scheme: Newton International Fellowships
Organisation: University of Cambridge
Dates: Jan 2015-Dec 2016
Summary: Collagens are the most abundant proteins in human body. They interact with other proteins to regulate the normal function of bone, cartilage, skin, eyes and cardiovascular and central nervous system. In their most widely distributed state, collagens form rope-like fibres that aggregate into a dense sponge-like network. Cells embed in this network through interaction with other proteins present on cell surface. This interaction is critical for numerous cellular functions. For example, other proteins degrade the collagen network surrounding cells to facilitate malignant cell growth during cancer progression. In a different context, exposure of blood proteins to collagen upon injury initiates clotting. This is life saving in the event of an external injury but fatal during clot induced blockage of arteries. Given such a breathtaking array of collagen function, understanding the molecular basis of its interaction to other proteins is key to developing suitable cures.
Due to the complexity of the collagen network, chemically designed polymers called peptides that mimic collagen are often used to study the collagen-protein interaction. Although mimics for some collagen types are readily available, design of mimics for the more widely distributed collagen types present in bone and skin is extremely challenging. So much so that a widely acceptable design of these mimics has eluded solution for nearly three decades.
Recently, I have developed a technology that can be used to readily prepare mimics of a wide variety of these abundant collagen types. Currently, I am studying the interaction one such mimic with a protein implicated in blood clotting. This mimic can be potentially used as a therapeutic drug to facilitate clotting during traumatic external injury or prevent it when cholesterol rich fatty deposits in the arteries break away and block them due to blood clotting.