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http://hdl.handle.net/1942/27421
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DC Field | Value | Language |
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dc.contributor.author | Simoes, Barbara | - |
dc.contributor.author | ADRIAENSENS, Peter | - |
dc.contributor.author | GUEDENS, Wanda | - |
dc.contributor.author | Goodwin, Paul | - |
dc.contributor.author | Mendes, Paula | - |
dc.date.accessioned | 2018-11-16T11:07:40Z | - |
dc.date.available | 2018-11-16T11:07:40Z | - |
dc.date.issued | 2018 | - |
dc.identifier.citation | RSC-XII Biological and Medicinal Chemistry Symposium for postgraduates, Cambridge, UK, 07/12/2018 | - |
dc.identifier.uri | http://hdl.handle.net/1942/27421 | - |
dc.description.abstract | Advances in biology research and clinical diagnosis require new biological inspired tools and technology platforms to measure, understand and control biological systems.1 Surface confined self-assembled monolayers (SAMs) of electro-switchable peptides have the capacity to regulate biomolecular interactions in response to an applied electrical potential.2-4 This study aims to understand the organization of charged peptides together with nanobody5 molecules (NbVCAM1) on a gold surface, in order to devise switchable surfaces with the capability to control the activity of NbVCAM1 binding to the human vascular cell adhesion hVCAM1, a molecule that attracts inflammatory cells, having an important role in the initiation of atherosclerosis.6-8 Contact Angle, Ellipsometry and X-ray Photon Spectroscopy (XPS) techniques have been used to characterize the surfaces with SAMs of charged peptides, namely, oligolysines, Cys-Lys(ε-Lys)4 (C5K) or Cys-Lys(ε-Lys)7 (C8K) on gold, individually or in the presence of the support molecule triethylene glycol mono-11-mercaptoundecyl ether (TEG11) and the NbVCAM1 nanobody. Results on mixed SAMs of C5K:TEG11 and C8K:TEG11 indicated the solution ratio of 40:1 as the optimal candidate for the switching studies. XPS results showed that the actual surface ratios are 1:(3±0.4) for C5K:TEG11 and 1:(3±0.2) for C8K:TEG11. Further characterization has been performed by Time-of-Flight Secondary Ion Mass Spectrometry (TOF-SIMS) to demonstrate the covalent binding of the NbVCAM1 nanobody to the gold surface. Electrochemistry Surface Plasmon Resonance (E-SPR) is being used to study the switching capabilities of these SAMs that include the NbVCAM1 at the surface. SPR results confirm the binding of hVCAM1 to the surface-tethered NbVCAM1 nanobody under open circuit (OC) conditions, with an electrical potential being able to switch the binding capabilities. | - |
dc.language.iso | en | - |
dc.title | Smart Switchable Biological Surfaces for On-Demand Biosensing | - |
dc.type | Conference Material | - |
local.bibliographicCitation.conferencedate | 07/12/2018 | - |
local.bibliographicCitation.conferencename | RSC-XII Biological and Medicinal Chemistry Symposium for postgraduates | - |
local.bibliographicCitation.conferenceplace | Cambridge, UK | - |
local.bibliographicCitation.jcat | C2 | - |
local.type.refereed | Refereed | - |
local.type.specified | Presentation | - |
item.contributor | Simoes, Barbara | - |
item.contributor | ADRIAENSENS, Peter | - |
item.contributor | GUEDENS, Wanda | - |
item.contributor | Goodwin, Paul | - |
item.contributor | Mendes, Paula | - |
item.fulltext | With Fulltext | - |
item.fullcitation | Simoes, Barbara; ADRIAENSENS, Peter; GUEDENS, Wanda; Goodwin, Paul & Mendes, Paula (2018) Smart Switchable Biological Surfaces for On-Demand Biosensing. In: RSC-XII Biological and Medicinal Chemistry Symposium for postgraduates, Cambridge, UK, 07/12/2018. | - |
item.accessRights | Restricted Access | - |
Appears in Collections: | Research publications |
Files in This Item:
File | Description | Size | Format | |
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PG symposium - abstract _17_09_2018_BSS_Switchable Surfaces (1).pdf Restricted Access | Conference material | 390.71 kB | Adobe PDF | View/Open Request a copy |
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