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Title: Studies on the understanding of collagenase inhibition through conformational changes in collagen
Researcher: Punitha V
Guide(s): Raghava rao J
Keywords: Bacterial collagenase
Collagenase inhibition
Collagen collagenase interaction
Upload Date: 28-Aug-2014
University: Anna University
Completed Date: 01/12/2012
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
Pagination: xxix, 717p.
Appears in Departments:Faculty of Technology

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01_title.pdfAttached File49.36 kBAdobe PDFView/Open
02_certificates.pdf3.94 MBAdobe PDFView/Open
03_abstract.pdf9.9 kBAdobe PDFView/Open
04_acknowledgement.pdf6.84 kBAdobe PDFView/Open
05_contents.pdf59.14 kBAdobe PDFView/Open
06_chapter1.pdf3.16 MBAdobe PDFView/Open
07_chapter2.pdf174.56 kBAdobe PDFView/Open
08_chapter3.pdf11.87 MBAdobe PDFView/Open
09_chapter4.pdf16.28 kBAdobe PDFView/Open
10_appendix.pdf10 kBAdobe PDFView/Open
11_references.pdf103.91 kBAdobe PDFView/Open
12_publications.pdf11.66 kBAdobe PDFView/Open
13_vitae.pdf7.29 kBAdobe PDFView/Open

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