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- W3014484976 abstract "Abstract One of the main problems in the development of immunosensors is to overcome the complexity of binding antibodies to the sensor surface. Most immobilizing methods lead to a random orientation of antibodies with a lower binding site density and immunoaffinity. In order to control the orientation of antibody immobilization, several resorc[4]arene derivatives were designed and synthesized. After the spectroscopic characterization of resorc[4]arene self‐assembled monolayers (SAMs) onto gold films, the surface coverage and the orientation of insulin antibody (Ab‐Ins) were assessed by a surface plasmon resonance (SPR) technique and compared with a random immobilization method. Experimental results combined with theoretical studies confirmed the dipole–dipole interaction as an important factor in antibody orientation and demonstrated the importance of the upper rim functionalization of resorcarenes. Accordingly, resorcarene 5 showed a major binding force towards Ab‐Ins thanks to the H‐bond interactions with the amine protein groups. Based on these findings, the resorcarene‐based immunosensor is a powerful system with improved sensitivity providing new insight into sensor development." @default.
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- W3014484976 date "2020-06-25" @default.
- W3014484976 modified "2023-10-16" @default.
- W3014484976 title "Site‐Directed Antibody Immobilization by Resorc[4]arene‐Based Immunosensors" @default.
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- W3014484976 doi "https://doi.org/10.1002/chem.202000989" @default.
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