Predicting the right spacing between protein immobilization sites on self-assembled monolayers to optimize ligand binding |
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Authors: | Javier Batista Perez Deependra Tyagi Mo Yang Loany Calvo Rolando Perez Ernesto Moreno Jinsong Zhu |
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Institution: | 1. National Center for Nanoscience and Technology, Beijing 100190, China;2. University of Chinese Academy of Sciences, Beijing 100190, China;3. Center of Molecular Immunology, Havana 16040, Cuba;4. Biotech Pharmaceutical, Beijing 100176, China |
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Abstract: | Self-assembled monolayers designed to immobilize capture antibodies are usually prepared using a mixture of functional and inactive linkers. Here, using low molar ratios (1:1 to 1:100) of the two linkers resulted in loss of binding capability of the anti-EGFR (epidermal growth factor receptor) antibody nimotuzumab, as assessed by surface plasmon resonance imaging. We then developed a simple theoretical model to predict the optimal surface density of the functional linker, taking into account the antibody size and linker diameter. A high (1:1000) dilution of the functional linker yielded the best results. As an advantage, this approach does not require chemical modification of the protein. |
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Keywords: | Self-assembled monolayer Protein immobilization Theoretical model Surface plasmon resonance Antibody Nimotuzumab |
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