Project information
Decoding Extracellular Protein–Protein Interactions with Synthetic Peptides

An average human body contains 1.5 kg of type I collagen—15% of all protein content. It is a structural scaffold and signaling hub, and plays a major role in fibrosis, with fibrotic diseases accounting for more than 45% of deaths in the developed world. Understanding the interactions of collagen I with other biomolecules is thus of utmost importance for biomedical research. Despite its abundance and importance, the interactome of collagen I remains poorly understood. As a major obstacle, collagen I cannot be isolated as a pure and homogenous protein, impeding systematic studies. In this project, we will recreate the sequence and triple-helical structure of collagen I via a library of self-assembled heterotrimeric peptide fragments. Towards this goal, we will develop short domains that will trimerize the collagen fragments in a defined spatial arrangement. Screening of the library against extracellular and cell-surface proteins will allow us to map the collagen I interactome, providing unprecedented insight into the biology of one of the most abundant proteins in the human body.