Materials Science

Partners in Healing

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Science  30 Sep 2011:
Vol. 333, Issue 6051, pp. 1803
DOI: 10.1126/science.333.6051.1803-c

The complexity of the interactions between growth factors, receptors, and the extracellular matrix makes it hard to replicate in vivo—like conditions when designing a clinical method for the delivery of growth factors. Some progress has been made by using multistaged controlled release methods or by covalently linking the growth factor to the matrix material, but, in these cases, the growth factors do not benefit from complex clustering effects that are needed to get the right cells to migrate, proliferate, and differentiate. Martino et al. devised a peptide that combined fibronectin fragments designed to cause integrin binding with fragments designed to cause growth factor binding. A third section contained coagulation factor XIIIa, which causes covalent immobilization of the fragments to the relevant part of a fibrin matrix. In comparison tests, with only one of the fibronectin fragments or with the two mixed together but not covalently linked, a synergistic healing effect was observed only when the two fragments were in close proximity on the same polypeptide chain. Enhanced regenerative healing was also observed in vivo when the engineered peptide was tested in a diabetic mouse model for chronic wounds and in a rat model for critical-size bone defects.

Sci. Transl. Med. 3, 100ra89 (2011).

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