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The pentapeptide NKISK affects collagen fibril interactions in a vertebrate tissue
Author(s) -
Dahners Laurence E.,
Lester Gayle E.,
Caprise Peter
Publication year - 2000
Publication title -
journal of orthopaedic research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.041
H-Index - 155
eISSN - 1554-527X
pISSN - 0736-0266
DOI - 10.1002/jor.1100180404
Subject(s) - fibril , pentapeptide repeat , chemistry , decorin , proteoglycan , collagen fibril , tendon , biophysics , fibronectin , extracellular matrix , electron microscope , vertebrate , microbiology and biotechnology , anatomy , peptide , biochemistry , biology , physics , gene , optics
Abstract The pentapeptide NKISK has been reported to inhibit the binding of decorin, a proteoglycan on the surface of collagen fibrils, to fibronectin, a tissue adhesion molecule. Because of our interest in fibril‐fibril binding as it relates to changes in length of ligament or tendon (during growth or contracture), we investigated the potential of this peptide to dissociate fibrils. The peptide permitted the release of intact fibrils into suspension for examination under the electron microscope (which has not previously been possible in mature vertebrate tissues).