Studies on the understanding of collagenase inhibition through conformational changes in collagen

Abstract

Understanding the mechanism of tanning through identification of forces involved in newlinecollagen stabilization in the presence of tanning agents is of profound interest In the present investigation, forces involved in collagen collagenase interaction and the role of amino acid chirality at the cleavage site of collagenase in collagen has been studied newlineThe effect of isopeptide bond on collagen structure and its stability against temperature and bacterial collagenase has been studied with the objective of understanding the role played by the charged functional groups present in collagen on collagen collagenase interaction Isopeptide bond formation in collagen resulted in an increase in thermal stability and decrease in collagenolytic activity with an increase in concentration of 1 Ethyl 3 carbodiimide hydrochloride The percentage inhibition of collagenase activity was found to be 78 for the 98 reduction of free amino group The formation of isopeptide bond between the side chains reduces the binding affinity of collagenase towards collagen by arresting the electrostatic interaction newline