Wednesday , 23 May 2018

Effect of Pepsin on Biochemical and Biophysical Studies of Collagen

R. Vani*1, S. Subathra1, R. Usha2, B. Kumar3, , B. Syed salman3
1Department of Biochemistry, Meenakshi College for Women, Chennai, Tamil Nadu
2Department of Biophysics,Central Leather Research Institute, Chennai, Tamil Nadu
3Department of Pharmaceutics,Ratnam Institute of Pharmacy, Pidathapolur, Nellore, Andhra Pradesh

One of the most important biomaterials under study throughout the world is collagen. Collagen is a large diverse family of fibrous proteins which accounts for about one quarter of total protein mass in our body it is a major extracellular and structural protein. It gives many different organs and tissues substantial stout and elastic properties. It is found in connective tissues such as tendons, hyaline cartilage, organic matrix bones, cornea of the eye, intervertebral disks, vitreous bodies, blood vessels, teeth, skin, placenta, and heart valves. Collagen plays a regulating role in developing tissues and cell type specific gene expression, differentiation of unspecialized cells and disease like cancer. Collagen occurs in the shape of fibres, ropes, straps, woven sheets, filtration membranes, supporting skeletal frame work and bearing materials. Collagen is a rod- shaped molecule of about 3,000 A0 long and 15A0 in diameter. Each turn of the helix is made up of nearly 3.3 amino acids and 2.9A0 height. From this study it was found that the shrinkage of rat tail tendon collagen fibre decreases as the concentration of pepsin increases the shrinkage optical micrographs of native RTT in water and 0.1% pepsin show the swelling behaviour of collagen. The reduction in the fibrillar stability indicates that naturally occurring bi/multifunctional cross links in the end region of the molecules. Which are responsible for the fibrillar stability are cleaved by pepsin. The denaturation temperature indicates the helix to coil transition in collagen. The kinetics of fibril formulation of native collagen shows the regular nucleation and growth phase. In the case of the kinetics of fibril formulation of pepsin treated collagen, there is irregular nucleation and growth phase.
Keywords: Collagen, Rat tail tendon, hierarchical organisation, Pepsin, Hydroxyproline.

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