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Synthesis of heterotrimeric collagen peptides containing the alpha 1 beta 1 integrin recognition site of collagen type IV

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http://pubman.mpdl.mpg.de/cone/persons/resource/persons78593

Saccà,  B.
Moroder, Luis / Bioorganic Chemistry, Max Planck Institute of Biochemistry, Max Planck Society;

http://pubman.mpdl.mpg.de/cone/persons/resource/persons78419

Moroder,  L.
Moroder, Luis / Bioorganic Chemistry, Max Planck Institute of Biochemistry, Max Planck Society;

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Saccà, B., & Moroder, L. (2002). Synthesis of heterotrimeric collagen peptides containing the alpha 1 beta 1 integrin recognition site of collagen type IV. Journal of Peptide Science, 8(5), 192-204.


Cite as: http://hdl.handle.net/11858/00-001M-0000-0010-6F54-A
Abstract
Collagen type IV provides a biomechanically stable scaffold into which the other constituents of basement membranes are incorporated, but it also plays an important role in cell adhesion. This occurs with collagen type IV mainly via the alpha1beta1 integrin, and the proposed epitope involved in this type of collagen/integrin interaction corresponds to a non- sequential R/Xaa/D motif, where the arginine and aspartate residues are provided by the alpha2 and alpha1 chains of the collagen molecule, respectively. Since the stagger of the three alpha chains in native collagen type TV is still unknown and different alignments of the chains lead to different spatial epitopes, two heterotrimeric collagen peptides containing the natural 457-469 sequences of the cell adhesion site were synthesized in which the single chains were assembled via disulfide bonds into the two most plausible alpha1alpha2alpha1' and alpha2alpha1alpha1' registers. The differentiated triple- helical stabilities of the two heterotrimers suggest a significant structural role of the chain register in collagen, although the binding to alpha1beta1 integrin is apparently less affected as indicated by preliminary experiments. Copyright (C) 2002 European Peptide Society and John Wiley Sons, Ltd.