Abstract
Yersina pestis, the bubonic plague bacterium, is coated with a polymeric protein hydrogel for protection from host defences. The protein, which is robust and non-stick, resembles structures found in many eukaryotic extracellular-matrix proteins. Cells grown on the natural polymer cannot adhere and grow poorly; however, when cell-adhesion motifs are inserted into the protein, the cells proliferate.
Highlights
Regenerative medicine demands the recreation of complex cell– cell and cell–matrix interactions observed in vivo[1] and has led to the development of artificial biomaterials to mimic the protein network in the extracellular matrix (ECM).[2,3]
Future developments would benefit from an economic supply of protein polymers which closely match the molecular structure of the natural material
Since Caf1 displays highly desirable properties that are difficult to design de novo into protein polymers, we investigated whether it could be a useful animal-free ECM substitute
Summary
Regenerative medicine demands the recreation of complex cell– cell and cell–matrix interactions observed in vivo[1] and has led to the development of artificial biomaterials to mimic the protein network in the extracellular matrix (ECM).[2,3] Future developments would benefit from an economic supply of protein polymers which closely match the molecular structure of the natural material. We reverse the “non-stick” phenotype by inserting a cell adhesion motif, express mixed polymers of different subunits and form hydrogels using a simple cross-linker. The expression of caf1, from its own temperature dependent promoter, was revealed by the presence of a flocculent layer (FL) above the cell pellet (CP) after centrifugation[14] (Figure 1C).
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.