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Peptide functionalized gold nanoparticles: the influence of pH on binding efficiency

Dixon, D, Hamilton, Jeremy, Harrison, Emma and Macias-Montero, Manuel (2017) Peptide functionalized gold nanoparticles: the influence of pH on binding efficiency. Nanotechnology, 28 (29). p. 295602. [Journal article]

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URL: http://iopscience.iop.org/article/10.1088/1361-6528/aa77ac/meta

DOI: 10.1088/1361-6528/aa77ac

Abstract

We report herein on the synthesis of mixed monolayer gold nanoparticles (AuNPs) capped with both polyethylene glycol (PEG) and one of three peptides. Either a receptor-mediated endocytosis peptide, an endosomal escape pathway (H5WYG) peptide or the Nrp-1 targeting RGD peptide (CRGDK) labeled with FITC. All three peptides have a thiol containing cysteine residue which can be used to bind the peptides to the AuNPs. In order to investigate the influence of pH on peptide attachment, PEGylated AuNPs were centrifuged, the supernatant removed, and the nanoparticles were then re-suspended in a range of pH buffer solutions above, below and at the respective isoelectric points of the peptides before co-functionalization. Peptide attachment was investigated using dynamic light scattering, Ultra-violet visible spectroscopy (UV/Vis), FTIR and photo luminescence spectroscopy. UV/Vis analysis coupled with protein assay results and photoluminescence of the FITC tagged RGD peptide concluded that a pH of ∼8 optimized the cysteine binding and stability, irrespective of the peptide used.

Item Type:Journal article
Keywords:gold nanoparticles
Faculties and Schools:Faculty of Computing & Engineering
Faculty of Computing & Engineering > School of Engineering
Research Institutes and Groups:Engineering Research Institute
Engineering Research Institute > Nanotechnology & Integrated BioEngineering Centre (NIBEC)
ID Code:38954
Deposited By: Dr Dorian Dixon
Deposited On:08 Jan 2018 11:17
Last Modified:08 Jan 2018 11:17

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