Two-dimensional membrane scaffold for the oriented immobilization of biosensing molecules

Publication date: Available online 9 November 2019Source: Biosensors and BioelectronicsAuthor(s): Masumi Iijima, Tsutomu Nakayama, Shun'ichi KurodaAbstractThe orientation and density of biosensing molecules on sensor chip should be precisely controlled to improve sensitivity and ligand-binding capacity. We previously developed a ∼30-nm bio-nanocapsule (ZZ-BNC), consisting of the hepatitis B virus envelope L protein fused with the tandem form of protein A-derived IgG Fc-binding Z domain (ZZ-L protein). This is used as a robust nanoparticle scaffold to enhance the sensitivity and ligand-binding capacity of IgGs and Fc-fused sensing molecules (Fc-fused receptors). However, due to their rigid particle structure, the surface density of ZZ-L proteins could not be optimized for biosensor functions, and useless ZZ-L proteins become stuck between ZZ-BNC and the sensor chip. Here, we have developed a planar lipid membrane embedded with ZZ-L micelles (ZZ-L membrane), which could modify the surface of any biosensor chip with a controlled density of ZZ-L proteins. Compared with ZZ-BNC, the sensitivity and ligand-binding capacity of IgGs were enhanced about 10-fold with the ZZ-L membrane. Furthermore, the immobilized IgGs could capture their respective antigens almost stoichiometrically, indicating that ZZ-L membrane is the most ideal scaffold for Fc-fused sensing molecules in terms of both clustering and oriented immobilization.
Source: Biosensors and Bioelectronics - Category: Biotechnology Source Type: research

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Source: Journal of Radioanalytical and Nuclear Chemistry - Category: Nuclear Medicine Source Type: research
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Source: Colloids and Surfaces B: Biointerfaces - Category: Biochemistry Source Type: research
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Source: Experimental and Therapeutic Medicine - Category: General Medicine Tags: Exp Ther Med Source Type: research
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Source: Journal of Clinical Gastroenterology - Category: Gastroenterology Tags: LIVER, PANCREAS & BILIARY TRACT: Original Articles Source Type: research
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Source: Acta Crystallographica Section E - Category: Chemistry Authors: Tags: crystal structure 2H-1,2,6-thiadiazine 1,1-dioxide hepatitis B HBV hydrogen bonding Hirshfeld surface analysis molecular docking study research communications Source Type: research
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Source: Human Vaccines and Immunotherapeutics - Category: Allergy & Immunology Authors: Source Type: research
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Source: Digestive Diseases and Sciences - Category: Gastroenterology Source Type: research
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Source: Journal of the American Academy of Dermatology - Category: Dermatology Authors: Source Type: research
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Source: Microbial Pathogenesis - Category: Infectious Diseases Source Type: research
Condition:   Hepatitis B Virus (HBV) Interventions:   Biological: ETV/TDF+T101 No.1;   Biological: ETV/TDF+T101 No.2;   Biological: ETV or TDF;   Biological: ETV/TDF+Peg-IFNα-2b Sponsor:   Tasly Tianjin Biopharmaceutical Co., Ltd. Not yet recruiting
Source: ClinicalTrials.gov - Category: Research Source Type: clinical trials
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