Backside-surface imprinting as a new strategy to generate specific plastic antibody materials
Author(s) -
Gustavo CabralMiranda,
Magnus Gidlund,
M. Goreti F. Sales
Publication year - 2014
Publication title -
journal of materials chemistry b
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.316
H-Index - 101
eISSN - 2050-7518
pISSN - 2050-750X
DOI - 10.1039/c3tb21740j
Subject(s) - template , materials science , biomolecule , polymer , covalent bond , imprinting (psychology) , monomer , dielectric spectroscopy , nanotechnology , layer (electronics) , electrochemistry , chemical engineering , electrode , chemistry , composite material , organic chemistry , biochemistry , engineering , gene
A backside protein-surface imprinting process is presented herein as a novel way to generate specific synthetic antibody materials. The template is covalently bonded to a carboxylated-PVC supporting film previously cast on gold, let to interact with charged monomers and surrounded next by another thick polymer. This polymer is then covalently attached to a transducing element and the backside of this structure (supporting film plus template) is removed as a regular "tape". The new sensing layer is exposed after the full template removal, showing a high density of re-binding positions, as evidenced by SEM. To ensure that the templates have been efficiently removed, this re-binding layer was cleaned further with a proteolytic enzyme and solution washout. The final material was named MAPS, as in the back-side reading of SPAM, because it acts as a back-side imprinting of this recent approach. It was able to generate, for the first time, a specific response to a complex biomolecule from a synthetic material. Non-imprinted materials (NIMs) were also produced as blank and were used as a control of the imprinting process. All chemical modifications were followed by electrochemical techniques. This was done on a supporting film and transducing element of both MAPS and NIM. Only the MAPS-based device responded to oxLDL and the sensing layer was insensitive to other serum proteins, such as myoglobin and haemoglobin. Linear behaviour between log(C, μg mL -1 ) versus charged tranfer resistance (R CT , Ω) was observed by electrochemical impedance spectroscopy (EIS). Calibrations made in Fetal Calf Serum (FCS) were linear from 2.5 to 12.5 μg mL -1 (R CT = 946.12 × log C + 1590.7) with an R-squared of 0.9966. Overall, these were promising results towards the design of materials acting close to the natural antibodies and applied to practical use of clinical interest.
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