Picture of boy being examining by doctor at a tuberculosis sanatorium

Understanding our future through Open Access research about our past...

Strathprints makes available scholarly Open Access content by researchers in the Centre for the Social History of Health & Healthcare (CSHHH), based within the School of Humanities, and considered Scotland's leading centre for the history of health and medicine.

Research at CSHHH explores the modern world since 1800 in locations as diverse as the UK, Asia, Africa, North America, and Europe. Areas of specialism include contraception and sexuality; family health and medical services; occupational health and medicine; disability; the history of psychiatry; conflict and warfare; and, drugs, pharmaceuticals and intoxicants.

Explore the Open Access research of the Centre for the Social History of Health and Healthcare. Or explore all of Strathclyde's Open Access research...

Image: Heart of England NHS Foundation Trust. Wellcome Collection - CC-BY.

Phosphatase responsive peptide surfaces

Zelzer, Mischa and McNamara, Laura E. and Scurr, David J. and Alexander, Morgan R. and Dalby, Matthew J. and Ulijn, Rein V. (2012) Phosphatase responsive peptide surfaces. Journal of Materials Chemistry, 22 (24). pp. 12229-12237. ISSN 0959-9428

Full text not available in this repository. Request a copy from the Strathclyde author


The development of interactive surfaces able to respond to biological cues is of interest for the development of next generation biomaterials. We report the design, synthesis and characterisation of an enzyme responsive peptide based surface whose chemical properties change upon catalytic action of alkaline phosphatase (AP). AP is a membrane-anchored enzyme involved in osteogenesis (bone formation), making it a suitable biomolecule to facilitate interactivity between the cell and the biomaterial surface. Surface analysis is used to follow dephosphorylation and a phosphate assay is used to determine the amount of phosphate removed by the enzyme. This analysis reveals significant differences in the dephosphorylation rate at the surface compared to that in solution. The ability of the surface to respond to native enzymes expressed by mesenchymal stem cells (MSCs) was indirectly explored by assessing the response of the cells to phosphorylated, non-phosphorylated and enzymatically dephosphorylated surfaces. No differences were found between the surfaces, suggesting that cell expressed enzymes are able to dephosphorylate the peptide surfaces rapidly. This work presents the first phosphatase responsive surfaces whose phosphorylation state can be altered by native enzymes provided by the cells.