دورية أكاديمية
Single‐Molecule Ex Situ Atomic Force Microscopy Allows Detection of Individual Antibody–Antigen Interactions on a Semiconductor Chip Surface
| العنوان: | Single‐Molecule Ex Situ Atomic Force Microscopy Allows Detection of Individual Antibody–Antigen Interactions on a Semiconductor Chip Surface |
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| المؤلفون: | Ming-Pei Lu, Ying-Ya Weng, Yuh-Shyong Yang |
| المصدر: | Advanced NanoBiomed Research, Vol 1, Iss 2, Pp n/a-n/a (2021) |
| بيانات النشر: | Wiley-VCH, 2021. |
| سنة النشر: | 2021 |
| المجموعة: | LCC:Biotechnology LCC:Medical technology |
| مصطلحات موضوعية: | antibody–antigen interactions, ex situ atomic force microscopy, hepatitis B virus X protein, IgG antibody, semiconductor chips, single-molecule detections, Biotechnology, TP248.13-248.65, Medical technology, R855-855.5 |
| الوصف: | Although in situ atomic force microscopy (AFM) allows single‐molecule detection of antibody–antigen binding, the practical applications of in situ AFM for disease diagnosis are greatly limited, due to its operational complexity and long operational times, including the execution time for the surface chemical/biological treatments in the equipped glass liquid cell. Herein, a method of graphically superimposed alignment that enables ex situ AFM analysis of an immobilized antibody at the same location on a semiconductor chip surface before and after incubation with its antigen is presented. All of the required chemical/biological treatments are executed feasibly using standard laboratory containers, allowing single‐molecule ex situ AFM detection to be conducted with great practicality, flexibility, and versatility. As an example, the analysis of hepatitis B virus X protein (HBx) and its IgG antibody is described. Using ex situ AFM, individual information on the topographical characteristics of the immobilized single and aggregated IgG antibodies on the chip surface is extracted and the data are analyzed statistically. Furthermore, in a statistical manner, the changes in AFM‐measured heights of the individual and aggregated IgG antibodies that occur as a result of changes in conformation upon formation of IgG–HBx complexes are investigated. |
| نوع الوثيقة: | article |
| وصف الملف: | electronic resource |
| اللغة: | English |
| تدمد: | 2699-9307 |
| Relation: | https://doaj.org/toc/2699-9307 |
| DOI: | 10.1002/anbr.202000035 |
| URL الوصول: | https://doaj.org/article/8c20638e2bee49c48e7a747fb9d2c77e |
| رقم الأكسشن: | edsdoj.8c20638e2bee49c48e7a747fb9d2c77e |
| قاعدة البيانات: | Directory of Open Access Journals |
Full Text Finder | تدمد: | 26999307 |
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| DOI: | 10.1002/anbr.202000035 |