AI Article Synopsis
- The study presents a method to create enzyme-responsive surfaces that activate cell adhesive RGD sequences through enzymatic hydrolysis of inactive precursors, allowing for on-demand functionality.
- These surfaces utilize poly(ethylene glycol) (PEG) monolayers attached to glass, offering a clear and versatile approach to peptide surface preparation using solid phase synthesis techniques.
- The effectiveness of this method is validated through surface analysis techniques and demonstrated with osteoblast cells, indicating potential applications in tissue engineering and biosensors.
Article Abstract
We report on the design, stepwise synthesis, and surface analysis of enzyme-responsive surfaces that present cell adhesive RGD sequences on-demand, that is, by enzymatic hydrolysis of inactive RGD containing precursors that carry cleavable steric blocking groups. These surfaces, incorporating poly(ethylene glycol) (PEG) monolayers coupled via epoxy silanes to glass, are functionalized via stepwise solid phase synthesis, presenting a versatile and straightforward approach to preparation of peptide surfaces. Successive amino acid coupling and deprotection steps using fluorenylmethoxycarbonyl (Fmoc) chemistry are verified using surface analysis with time-of-flight secondary-ion mass spectrometry (ToF-SIMS) and X-ray photoelectron spectroscopy (XPS). Exposure of surfaces to elastase results in activation of cell binding ligands as demonstrated using osteoblast cells. These surfaces may have applications in spatiotemporally controlled attachment of cells as relevant for three-dimensional tissue engineering scaffolds and cell-based biosensors.
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| http://dx.doi.org/10.1021/la900376h | DOI Listing |
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