Disease antigens detection by silicon nanowires with the efficiency optimization of their antibodies on a chip.
Biosens Bioelectron
; 141: 111209, 2019 Sep 15.
Article
em En
| MEDLINE
| ID: mdl-31357174
Enhancing the efficiency of antibody protein immobilized on a silicon nanowire-based chip for their antigens detection is reported. An external electric field (EEF) is applied to direct the orientation of antibodies during their immobilization on a chip. Atomic force microscopy (AFM) is used to measure the binding forces between immobilized antibody and targeting antigen under the influence of EEF at different angles. The maximum binding force under a specific angle (optimal angle; oa) of EEF (maxEEFoa) implies the optimal orientation of the antibodies on the chip. In this report, two different cancer carcinoembryonic antigen (CEA)-related cell adhesion molecules 5 (CEACAM5) & 1 (CEACAM1) were used for the examples of disease antigen detection. maxEEFoa of anti-CEACAM5 or anti-CEACAM1 immobilized on a general chip was firstly determined. Spectroscopy of AFM revealed that both binding forces were the largest ones with their antigens when maxEEFoa was applied as compared with no or other angles of EEF. These antibody proteins accompanied with the application of EEF were secondly immobilized on silicon-nanowires (nâ¯=â¯1000) and the field effects were measured (∆I) as their target antigens were approached. Results showed that ∆I was the largest ones when maxEEFoas (225°/270° and 135°/180° for anti-CEACAM5 and anti-CEACAM1, respectively) were applied as compared with other angles of EEF. These observations imply that the silicon nanowires together with the application of maxEEFoa as detection tools could be applied for the cancer diagnostics in the future.
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Base de dados:
MEDLINE
Assunto principal:
Silício
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Técnicas Biossensoriais
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Antígeno Carcinoembrionário
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Antígenos CD
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Moléculas de Adesão Celular
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Nanofios
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Anticorpos Imobilizados
Tipo de estudo:
Diagnostic_studies
Limite:
Humans
Idioma:
En
Ano de publicação:
2019
Tipo de documento:
Article