ハイアフィニティ分子間相互作用解析システム
KinExA 4000

KinExA シリーズ：資料ダウンロード

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• KinExA Advantage: A comparison of biosensors for K_d analysis（英語）

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ニュースレター

Sapidyne Instruments社が毎年発刊しているニュースレターです。KinExAに関する様々な有用な情報が掲載されています。

参照論文

Affinity & Kinetic Measurements: ​

KinExA technology overview:

• Wani T.A., et al. 2016.
  New analytical application of antibody-based biosensor in estimation of thyroid-stimulating hormone in serum. 
  Bioanalysis 10.4155/bio-2015-0034.  https://www.ncbi.nlm.nih.gov/pubmed/26978548 

• Glass T.R., Winzor D.J. 2014.
  Confirmation of the validity of the current characterization of immunochemical reactions by kinetic exclusion assay. 
  Anal Biochem 456: 38-42.  http://www.ncbi.nlm.nih.gov/pubmed/24751468 

• Bee C., et al. 2012.
  Exploring the dynamic range of the kinetic exclusion assay in characterizing antigen-antibody interactions. 
  PLOS ONE 7(4): e36261.  http://www.ncbi.nlm.nih.gov/pubmed/22558410

• Darling R.J. and Brault P.A. 2004.
  Kinetic exclusion assay technology: characterization of molecular interactions. 
  Assay and Drug Dev Tech 2(6): 647-657.  http://www.ncbi.nlm.nih.gov/pubmed/15674023

KinExA’s role in drug discovery:

• Danial M, et al. 2017.
  Site-Specific Polymer Attachment to HR2 Peptide Fusion Inhibitors against HIV-1 Decreases Binding Association Rates and Dissociation Rates Rather Than Binding Affinity. 
  Bioconjug Chem. 10.1021/acs.bioconjchem.6b00540. https://www.ncbi.nlm.nih.gov/pubmed/?term=10.1021%2Facs.bioconjchem.6b00540

• Kariolis MS, et al. 2017.
  Inhibition of the GAS6/AXL pathway augments the efficacy of chemotherapies. 
  J Clin Invest. 10.1172/JCI85610.  https://www.ncbi.nlm.nih.gov/pubmed/?term=10.1172%2FJCI85610

• Fan Y., et al. 2016.
  Immunological Characterization and Neutralizing Ability of Monoclonal Antibodies Directed Against Botulinum Neurotoxin Type H. 
  The Journal of Infectious Diseases 15;213(10):1606-14.  https://www.ncbi.nlm.nih.gov/pubmed/26936913

• Köck, K., et al. 2015.
  Preclinical development of AMG 139, a human antibody specifically targeting IL-23. 
  British Journal of Pharmacology 172:159-172.  http://www.ncbi.nlm.nih.gov/pubmed/25205227

• Tabrizi M.A., et al. 2009.
  Translational strategies for development of monoclonal antibodies from discovery to the clinic.
  Drug Discov Today 14(5/6): 298-305.  http://www.ncbi.nlm.nih.gov/pubmed/19152840

Significance of “solution phase” measurements to unmodified molecules:

• Tigue NJ, et al. 2017.
  MEDI1873, a potent, stabilized hexameric agonist of human GITR with regulatory T-cell targeting potential. 
  Oncoimmunology.10.1080/2162402X.2017.1280645.  https://www.ncbi.nlm.nih.gov/pubmed/?term=10.1080%2F2162402X.2017.1280645

• Kusano-Arai 0., et al. 2016.
  Kinetic exclusion assay of monoclonal antibody affinity to the membrane protein Roundabout 1 displayed on baculovirus.
  Anal Biochem.10.1016/j.ab.2016.04.004.  https://www.ncbi.nlm.nih.gov/pubmed/27095060

• Blake R.C., Li X., Blake D.A. 2007.
  Covalent and noncovalent modifications induce allosteric binding behavior in a monoclonal antibody. 
  Biochemistry 46: 1573-1586.  http://www.ncbi.nlm.nih.gov/pubmed/17279622

Comparison to SPR:

• Fleming JK, Wojciak JM. 2017.
  Measuring Sphingosine-1-Phosphate: Protein Interactions with the Kinetic Exclusion Assay.
  Methods Mol Biol. 10.1007/7651_2017_5.  https://www.ncbi.nlm.nih.gov/pubmed/28349502

• Abdiche YN. et al. 2016.
  Assessing kinetic and epitopic diversity across orthogonal monoclonal antibody generation platforms. 
  MAbs. 10.1080/19420862.2015.1118596.  https://www.ncbi.nlm.nih.gov/pubmed/?term=10.1080%2F19420862.2015.1118596

• Kusano-Arai 0., et al. 2016.
  Kinetic exclusion assay of monoclonal antibody affinity to the membrane protein Roundabout 1 displayed on baculovirus. 
  Anal Biochem.10.1016/j.ab.2016.04.004.  https://www.ncbi.nlm.nih.gov/pubmed/27095060

• Drake A.W., et al. 2012.
  Biacore surface matrix effects on the binding kinetics and affinity of an antigen/antibody complex. 
  Anal Biochem. 429(1):58-69.  http://www.ncbi.nlm.nih.gov/pubmed/22766435

Sensitivity to measure tight binders:

• Abdiche YN. et al. 2016.
  Assessing kinetic and epitopic diversity across orthogonal monoclonal antibody generation platforms. 
  MAbs. 10.1080/19420862.2015.1118596.  https://www.ncbi.nlm.nih.gov/pubmed/?term=10.1080%2F19420862.2015.1118596

• Owyang A.M., et al. 2011.
  XOMA 052, a potent, high-affinity monoclonal antibody for the treatment of IL-1B-mediated diseases. 
  mAbs 3(1): 49-60.  http://www.ncbi.nlm.nih.gov/pubmed/21048425

• Champagne K., Shishido A., Root M.J. 2009.
  Interaction of HIV-1 inhibitory peptide T20 with gp41 N-HR coiled coil. 
  J Biol Chem 284: 3619-3627.  http://www.ncbi.nlm.nih.gov/pubmed/19073602

• Kostenuik P.J., et al. 2009.
  Denosumab, a fully human monoclonal antibody to RANKL, inhibits bone resorption and increases BMD in knock-in mice that express chimeric (murine/human) RANKL.
   J Bone Miner Res 24: 182-195.  http://www.ncbi.nlm.nih.gov/pubmed/19016581

• Luginbuhl B., et al. 2006.
  Directed evolution of an anti-prion protein scFv fragment to an affinity of 1 pM and its structural interpretation. 
  J Mol Biol 363: 75-97.  http://www.ncbi.nlm.nih.gov/pubmed/16962610

• Rathanaswami P., et al. 2005.
  Demonstration of an in vivo generated sub-picomolar affinity fully human monoclonal antibody to interleukin-8. 
  Biochem Biophys Res Comm 334: 1004-1013.  http://www.ncbi.nlm.nih.gov/pubmed/16038881

Reverse assay techniques:

• Razai A., et al. 2005.
  Molecular evolution of antibody affinity for sensitive detection of botulinum neurotoxin type A.
  J Mol Biol 351: 158-169.  http://www.ncbi.nlm.nih.gov/pubmed/16002090

Whole cell binding techniques:

• Bedinger, D., et al. 2015.
  Differential pathway coupling of activated insulin receptor drives signaling selectivity by XmetA, an allosteric partial agonist antibody. 
  J Pharmacol Exp Ther353(1):35-43.  http://www.ncbi.nlm.nih.gov/pubmed/25613982

• Rathanaswami P., Babcook J., Gallo M. 2008.
  High-affinity binding measurements of antibodies to cell-surface-expressed antigens. 
  Anal Biochem 373: 52-60.  http://www.ncbi.nlm.nih.gov/pubmed/17910940

• Xie L., et al. 2005.
  Measurement of the functional affinity constant of a monoclonal antibody for cell surface receptors using kinetic exclusion fluorescence immunoassay. 
  J Immunol Methods 304: 1-14.  http://www.ncbi.nlm.nih.gov/pubmed/16098983

Unpurified antigens:

• Wani T.A., et al. 2016.
  Analytical Application of Flow Immunosensor in Detection of Thyroxine and Triiodothyronine in Serum. 
  Assay Drug Dev Technol.14(9):535-542.  https://www.ncbi.nlm.nih.gov/pubmed/27801595

• Bee C., et al. 2013.
  Determining the binding affinity of therapeutic monoclonal antibodies towards their native unpurified antigens in human serum. 
  PLOS ONE 8(11): e80501.  http://www.ncbi.nlm.nih.gov/pubmed/24223227

• Fujino, Y., et al. 2012.
  Robust in vitro affinity maturation strategy based on interface-focused high-throughput mutational scanning. 
  Biochem Biophys Res Commun 4283:395-400.  http://www.ncbi.nlm.nih.gov/pubmed/23103372

• Rathanaswami P., et al. 2011.
  Kinetic analysis of unpurified native antigens available in very low quantities and concentrations. 
  Anal Biochem 414: 7-13.  http://www.ncbi.nlm.nih.gov/pubmed/21371417

Other interesting studies:

• Li X., Kaattari S.L., Vogelbein M.A., Vadas G.G., Unger M.A., 2016.
  A highly sensitive monoclonal antibody based biosensor for quantifying 3-5 ring polycyclic aromatic hydrocarbons (PAHs) in aqueous environmental samples. 
  Sens Biosensing Res. 7:115-120.  https://www.ncbi.nlm.nih.gov/pubmed/26925369

• Lou J., et al. 2010.
  Affinity maturation of human botulinum neurotoxin antibodies by light chain shuffling via yeast mating. 
  Protein Eng Des Sel 23(4): 311-319.  http://www.ncbi.nlm.nih.gov/pubmed/20156888

• Kahle K.M., Steger H.K., Root M.J. 2009.
  Asymmetric deactivation of HIV-1 gp41 following fusion inhibitor binding. 
  PLOS Path 5(11): 1-11.  http://www.ncbi.nlm.nih.gov/pubmed/19956769

• Nowakowski A., et al. 2002.
  Potent neutralization of botulinum neurotoxin by recombinant oligoclonal antibody. 
  Proc Natl Acad Sci 99: 11346-11350.  http://www.ncbi.nlm.nih.gov/pubmed/1217743

Immunoassay Techniques:

• Darwish I.A., et al. 2013.
  Kinetic-exclusion analysis-based immunosensors versus enzyme-linked immunosorbent assays for measurement of cancer markers in biological specimens. 
  Talanta 111: 13-19.  http://www.ncbi.nlm.nih.gov/pubmed/23622520​

• Prieto-Simon B., Miyachi H., Karube I., Saiki H. 2010.
  High-sensitive flow-based kinetic exclusion assay for okadaic acid assessment in shellfish samples. 
  Biosens Bioelectron 25: 1395-1401.  http://www.ncbi.nlm.nih.gov/pubmed/19939663

• Sasaki K., Oguma S., Namiki Y., Ohmura N. 2009.
  Monoclonal antibody to trivalent chromium chelate complex and its application to measurement of the total chromium concentration. 
  Anal Chem 81: 4005-4009.  http://www.ncbi.nlm.nih.gov/pubmed/19438265

• Glass T.R., Ohmura N., Saiki H. 2007.
  Least detectable concentration and dynamic range of three immunoassay systems using the same antibody. 
  Anal Chem 79: 1954-1960.  http://www.ncbi.nlm.nih.gov/pubmed/17256970

• Bromage E.S., et al. 2007.
  The development of a real-time biosensor for the detection of trace levels of trinitrotoluene (TNT) in aquatic environments. 
  Biosens Bioelectron 22: 2532-2538.  http://www.ncbi.nlm.nih.gov/pubmed/17088054

• Sasaki K., Glass T.R., Ohmura N. 2005.
  Validation of accuracy of enzyme-linked immunosorbent assay in hybridoma screening and proposal of an improved screening method. 
  Anal Chem 77: 1933-1939.  http://www.ncbi.nlm.nih.gov/pubmed/15801721

• Glass T.R., et al. 2004.
  Use of excess solid-phase capacity in immunoassays: advantages for semicontinuous, near-real-time measurements and for analysis of matrix effects. 
  Anal Chem76: 767-772.  http://www.ncbi.nlm.nih.gov/pubmed/14750874

• Ohmura N., Lackie S., Saiki H. 2001.
  An immunoassay for small analytes with theoretical detection limits. 
  Anal Chem 73: 3392-3399.  http://www.ncbi.nlm.nih.gov/pubmed/11476240