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n nature, molecules spontaneously self-assemble to form stable assemblies, creating for example, proteins and lipid structures
in cells. In recent years, this process has been exploited to produce hydrogels based on amino acids, the building blocks of
proteins. These supramolecular hydrogels can be based on β-sheets, α-helices and random coils. With 20 natural amino acids
to use as the building blocks, and an infinite number of synthetic analogues, with various properties, a wide range of gels with
varying physical and chemical properties can be produced. The high water content, porosity, potential for cellular remodeling
and the nanofibrous architecture has resulted in peptide hydrogels being labelled as extracellular matrix (ECM) mimics, with the
potential for numerous biological applications.
We have produced nanofibrous peptide hydrogels based on tripeptide and octapeptide systems for skin, cartilage and
intervertebral disc cell culture and tissue engineering. Cell viability, proliferation and matrix production suggest these gels can
maintain viable environments for use as 3D cell culture systems and tissue engineering applications.
Julie Gough completed her Ph.D. at The University of Nottingham, UK and postdoctoral studies at The University of Nottingham and at Imperial
College London. Julie is currently Reader in Biomaterials and Tissue Engineering at the University of Manchester, UK and has published more than
60 papers in reputed journals
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