TY  - JOUR
A1  - Federico, Stefania
A1  - Pierce, Benjamin F.
A1  - Piluso, Susanna
A1  - Wischke, Christian
A1  - Lendlein, Andreas
A1  - Neffe, Axel T.
T1  - Design of Decorin-Based Peptides That Bind to CollagenI and their Potential as Adhesion Moieties in Biomaterials
JF  - Angewandte Chemie : a journal of the Gesellschaft Deutscher Chemiker ; International edition
N2  - Mimicking the binding epitopes of protein-protein interactions by using small peptides is important for generating modular biomimetic systems. A strategy is described for the design of such bioactive peptides without accessible structural data for the targeted interaction, and the effect of incorporating such adhesion peptides in complex biomaterial systems is demonstrated. The highly repetitive structure of decorin was analyzed to identify peptides that are representative of the inner and outer surface, and it was shown that only peptides based on the inner surface of decorin bind to collagen. The peptide with the highest binding affinity for collagenI, LHERHLNNN, served to slow down the diffusion of a conjugated dye in a collagen gel, while its dimer could physically crosslink collagen, thereby enhancing the elastic modulus of the gel by one order of magnitude. These results show the potential of the identified peptides for the design of biomaterials for applications in regenerative medicine.
KW  - biomaterials
KW  - collagen
KW  - gels
KW  - peptides
KW  - protein-protein interactions
Y1  - 2015
U6  - https://doi.org/10.1002/anie.201505227
SN  - 1433-7851
SN  - 1521-3773
VL  - 54
IS  - 37
SP  - 10980
EP  - 10984
PB  - Wiley-VCH
CY  - Weinheim
ER  -