Supramolecular modification of a sequence-controlled collagen-mimicking polymer

Sergio Spaans, Peter Paul K.H. Fransen, Maaike J.G. Schotman, Ruben van der Wulp, René P.M. Lafleur, Sebastiaan G.J.M. Kluijtmans, Patricia Y.W. Dankers (Corresponding author)

Research output: Contribution to journalArticleAcademicpeer-review

12 Citations (Scopus)
171 Downloads (Pure)


Structurally and functionally well-defined recombinant proteins are an interesting class of sequence-controlled macromolecules to which different crosslinking chemistries can be applied to tune their biological properties. Herein, we take advantage of a 571-residue recombinant peptide based on human collagen type I (RCPhC1), which we functionalized with supramolecular 4-fold hydrogen bonding ureido-pyrimidinone (UPy) moieties. By grafting supramolecular UPy moieties onto the backbone of RCPhC1 (UPy-RCPhC1), increased control over the polymer structure, assembly, gelation, and mechanical properties was achieved. In addition, by increasing the degree of UPy functionalization on RCPhC1, cardiomyocyte progenitor cells were cultured on "soft" (?26 kPa) versus "stiff" (?68-190 kPa) UPy-RCPhC1 hydrogels. Interestingly, increased stress fiber formation, focal adhesions, and proliferation were observed on stiffer compared to softer substrates, owing to the formation of stronger cell-material interactions. In conclusion, a bioinspired hydrogel material was designed by a combination of two well-known natural components, i.e., a protein as sequence-controlled polymer and UPy units inspired on nucleobases.

Original languageEnglish
Pages (from-to)2360-2371
Number of pages12
Issue number6
Publication statusPublished - 10 Jun 2019


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