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Coiled coil peptide-functionalized surfaces for reversible molecular binding.

Minelli, C; Liew, J X*; Muthu, M*; Andresen, H* (2013) Coiled coil peptide-functionalized surfaces for reversible molecular binding. Soft Matter, 9 (20). pp. 5119-5124.

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Abstract

We have studied the conformational and self assembly properties of de novo peptides derived from the structure of the yeast transcriptional activator GCN4 in solution and on surfacesand showed how the pH and the polarity of the solvent control peptide conformation. The peptides self-assembled in a coiled coil structure at acidic pH whereas they disassembled at alkaline pH values. Solvent polarity infuenced the peptide ability of forming alpha-helixes. We have used these properties to control the peptide packing density on gold surfaces, and demonstrated with functionalised gold nanoparticles that such peptide-engineered surfaces can be used for reversible molecular binding.

Item Type: Article
Keywords: Coiled-coils, QCM-D, SPR, molecular binding
Subjects: Nanoscience
Nanoscience > Surface and Nanoanalysis
Identification number/DOI: 10.1039/c3sm50379h
Last Modified: 02 Feb 2018 13:14
URI: http://eprintspublications.npl.co.uk/id/eprint/5832

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