Label-Free Kinetic Analysis of an Antibody–Antigen Interaction Using Biolayer Interferometry

2015 ◽  
pp. 165-182 ◽  
Author(s):  
Sriram Kumaraswamy ◽  
Renee Tobias
Keyword(s):  
Kinetic Analysis ◽  
Label Free ◽  
Biolayer Interferometry ◽  
Antigen Interaction

Label-Free Optical Detection of Protein Antibody–Antigen Interaction on Au Capped Porous Anodic Alumina Layer Chip

2008 ◽  
Vol 47 (2) ◽  
pp. 1351-1354 ◽  
Author(s):  
Do-Kyun Kim ◽  
Kagan Kerman ◽  
Shohei Yamamura ◽  
Young-Soo Kwon ◽  
Yuzuru Takamura ◽  
...  
Keyword(s):  
Optical Detection ◽  
Anodic Alumina ◽  
Porous Anodic Alumina ◽  
Label Free ◽  
Alumina Layer ◽  
Antigen Interaction

Label-Free Detection of Leptin Antibody-Antigen Interaction by Using LSPR-Based Optical Biosensor

2011 ◽  
Vol 11 (5) ◽  
pp. 4188-4193 ◽  
Author(s):  
Do-Kyun Kim ◽  
Tae Jung Park ◽  
Eiichi Tamiya ◽  
Sang Yup Lee
Keyword(s):  
Optical Biosensor ◽  
Label Free ◽  
Label Free Detection ◽  
Antigen Interaction

Label-Free Detection of Biomolecular Interactions Using BioLayer Interferometry for Kinetic Characterization

2009 ◽  
Vol 12 (8) ◽  
pp. 791-800 ◽  
Author(s):  
Joy Concepcion ◽  
Krista Witte ◽  
Charles Wartchow ◽  
Sae Choo ◽  
Danfeng Yao ◽  
...  
Keyword(s):  
Biomolecular Interactions ◽  
Kinetic Characterization ◽  
Label Free ◽  
Biolayer Interferometry ◽  
Label Free Detection

scholarly journals Kinetic Analysis of Glycoprotein–Lectin Interactions by Label-Free Internal Reflection Ellipsometry

2008 ◽  
Vol 4 (1-2) ◽  
pp. 37-46 ◽  
Author(s):  
David W. Ralin ◽  
Shane C. Dultz ◽  
Judd E. Silver ◽  
Jeffrey C. Travis ◽  
Majlinda Kullolli ◽  
...  
Keyword(s):  
Kinetic Analysis ◽  
Internal Reflection ◽  
Label Free

scholarly journals 2LTRZFP Interacts Specifically to HIV-1 DNA without Off-Target Effects as Determined by Biolayer Interferometry

Biosensors ◽  
2021 ◽  
Vol 11 (3) ◽  
pp. 76
Author(s):  
Koollawat Chupradit ◽  
Weeraya Thongkum ◽  
On-anong Juntit ◽  
Kanokporn Sornsuwan ◽  
Chatchai Tayapiwatana
Keyword(s):  
Specific Binding ◽  
Enzyme Linked Immunosorbent Assay ◽  
Supt1 Cell ◽  
Label Free ◽  
Dna Interactions ◽  
Biolayer Interferometry ◽  
Cellular Processes ◽  
Hiv 1 ◽  
2Ltr Circle ◽  
Target Effects

Protein and DNA interactions are crucial for many cellular processes. Biolayer Interferometry (BLI) is a label-free technology for determining kinetic biomolecular interactions with high accuracy results. In the present study, we determined the kinetic binding of a zinc finger scaffold, 2LTRZFP, which formerly constructed the interfering effect on HIV-1 integration process using BLI. The competitive Enzyme-linked immunosorbent assay (ELISA) was used to initially show the specific binding of 2LTRZFP. The percentages of inhibition were 62% and 22% in double-stranded 2LTR (ds2LTR) and irrelevant DNA (dsNeg), respectively. Consequently, the binding affinity of 2LTRZFP against ds2LTR target analyzed by BLI was 40 nM, which is stronger than the interaction of HIV-1 integrase (IN) enzyme to the 2LTR circle junction. Additionally, the 2LTRZFP did not interact with the genomic DNA extracted from SupT1 cell line. This result indicates that 2LTRZFP did not exhibit off-target effects against human genome. The knowledge obtained from this study supports the prospect of using 2LTRZFP in HIV-1 gene therapy.

Kinetic analysis of a high-affinity antibody/antigen interaction performed by planar waveguide fluorescence immunosensor

RSC Advances ◽  
2016 ◽  
Vol 6 (17) ◽  
pp. 13837-13845 ◽  
Author(s):  
Hongli Guo ◽  
Xiaohong Zhou ◽  
Yan Zhang ◽  
Chunmei Gu ◽  
Baodong Song ◽  
...  
Keyword(s):  
Kinetic Analysis ◽  
Planar Waveguide ◽  
Biomolecular Interactions ◽  
Optical Biosensors ◽  
High Affinity ◽  
Antigen Interaction

Methods based on optical biosensors for the investigation of biomolecular interactions between high-affinity antibodies and antigens has advanced over the last years.

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