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Welcome to the Collagen Toolkits Web Resource

MMP-1(E200A) bound to a triple-helical collagen peptideCollagen Toolkits are sets of overlapping triple-helical peptides (THPs) encompassing the entire Col domains of human collagens II and III. These peptides can be arrayed in 96-well plates and used to map binding sites. When specific sites have been located, then a subset of peptides can be made that will pinpoint the exact binding motif within the collagen, allowing specific THPs to be made as research reagents.

Collagen II and III were selected for this exercise because they are homotrimeric, and self-assembling, accurately-folding peptides are straightforward to synthesise and use. The substantial homology between collagen II (alpha1) and collagen I (alpha1) chains, means that the Toolkits can provide useful insight into binding sites in collagen I and others as well as in the designated collagen.

Examples of the way we have used the Toolkits to map and then pinpoint binding sites in collagens II and III are provided by integrin alpha1beta1, integrin alpha2beta1, platelet Glycoprotein VI (GpVI), von Willebrand factor (VWF), discoidin domain receptor 2 (DDR2) and other species. See links on this page to our published, completed studies.

The underlying purpose of this website is to offer a gateway to those who have a collagen-binding material (e.g. a collagen receptor, or another collagen-binding matrix component) who wish to locate its binding site within the fibrillar human collagens.


Peptide Chemists

Arkadiusz Bonna, SRA on BHF Programme Grant.

      Primary responsibility for managing the Toolkits, and in supplying peptides to the community.

Jean-Daniel Malcor, RA on BHF Special Project Grant.

     Primary responsibility for making integrin ligands, and for conjugating peptides to scaffolds for regenerative medicine.

Abhishek Jalan, Newton International Fellow, now University of Bayreuth, Germany.

     Unique skill set is in making heterotrimeric peptides using charge-complementarity to direct the register of the strands.