Type IX collagen NC1 domain peptides can trimerize in vitro without forming a triple helix

Diane E. Mechling, Jay E. Gambee, Nicholas P. Morris, Lynn Y. Sakai, Douglas R. Keene, Richard Mayne, Hans Peter Bächinger

Research output: Contribution to journalArticle

29 Scopus citations

Abstract

Synthetic peptides of the three chains of type IX collagen consisting of the carboxyl-terminal end of the COL1 domain and the complete NC1 domain were characterized by circular dichroism spectroscopy and analyzed for their ability to assemble into trimers. In vitro association and oxidation result in disulfide-linked oligomers as shown by molecular sieve chromatography and SDS-polyacrylamide electrophoresis. Whereas the individual peptides show a tendency to self-associate, when an equimolar amount of the three peptides was oxidized, a heterotrimer of the three chains was observed. This heterotrimer is recognized by a monoclonal antibody against the disulfide- linked NC1 domain of chicken type IX collagen, indicating the correct formation of the disulfide bonds. Circular dichroism measurements show that under the association conditions used, a triple helix does not form between the chains. These results indicate that these peptides contain all the necessary information for chain selection and assembly.

Original languageEnglish (US)
Pages (from-to)13781-13785
Number of pages5
JournalJournal of Biological Chemistry
Volume271
Issue number23
DOIs
StatePublished - Jun 25 1996

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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    Mechling, D. E., Gambee, J. E., Morris, N. P., Sakai, L. Y., Keene, D. R., Mayne, R., & Bächinger, H. P. (1996). Type IX collagen NC1 domain peptides can trimerize in vitro without forming a triple helix. Journal of Biological Chemistry, 271(23), 13781-13785. https://doi.org/10.1074/jbc.271.23.13781