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Article ; Online: Targeted instant immunity.

Meares, Claude F

2009 Volume 27, Issue 5, Page(s) 452–453

MeSH term(s)	Animals ; Antibodies/immunology ; Haptens/immunology ; Immunotherapy ; Mice ; Neoplasms/immunology ; Neoplasms/therapy
Chemical Substances	Antibodies ; Haptens
Language	English
Publishing date	2009-05-08
Publishing country	United States
Document type	News
ZDB-ID	1311932-1
ISSN	1546-1696 ; 1087-0156
ISSN (online)	1546-1696
ISSN	1087-0156
DOI	10.1038/nbt0509-452
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Article: The chemistry of irreversible capture.

Meares, Claude F

Advanced drug delivery reviews

2008 Volume 60, Issue 12, Page(s) 1383–1388

Abstract: The specific recognition and binding of biological molecules by antibodies is fundamentally important. Natural antibodies are multivalent, having at least two identical ligand-binding sites; this permits them to bind tightly at cell surfaces, which ... ...

Abstract	The specific recognition and binding of biological molecules by antibodies is fundamentally important. Natural antibodies are multivalent, having at least two identical ligand-binding sites; this permits them to bind tightly at cell surfaces, which present multiple copies of their target ligands. Antibodies that bind to soluble monovalent ligands, such as most small molecules, do not share this multivalent advantage. Nor do engineered fragments of antibodies, such as single-chain Fv proteins or Fab fragments, which generally possess only a single ligand-binding site. Engineered monovalent antibody/ligand pairs that retain the binding specificity of the antibody, but do not dissociate, are promising components of new delivery systems. These are based on a combination of genetic manipulation of the protein and chemical synthesis of appropriate ligands, examples of which are reviewed here.
MeSH term(s)	Affinity Labels/chemistry ; Antibodies/administration & dosage ; Antibody Affinity ; Chelating Agents/chemistry ; Drug Delivery Systems ; Protein Engineering
Chemical Substances	Affinity Labels ; Antibodies ; Chelating Agents
Language	English
Publishing date	2008-04-24
Publishing country	Netherlands
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	639113-8
ISSN	1872-8294 ; 0169-409X
ISSN (online)	1872-8294
ISSN	0169-409X
DOI	10.1016/j.addr.2008.04.010
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Article ; Online: Introduction to gene silencing and delivery.

Meares, Claude F / Yokoyama, Masayuki

Accounts of chemical research

2012 Volume 45, Issue 7, Page(s) 959–960

MeSH term(s)	Gene Expression Regulation ; Gene Silencing ; Gene Transfer Techniques ; Polymers/chemistry ; Proteins/genetics ; Proteins/metabolism
Chemical Substances	Polymers ; Proteins
Language	English
Publishing date	2012-07-17
Publishing country	United States
Document type	Editorial
ZDB-ID	1483291-4
ISSN	1520-4898 ; 0001-4842
ISSN (online)	1520-4898
ISSN	0001-4842
DOI	10.1021/ar300157k
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Article ; Online: Combination of isothermal titration calorimetry and time-resolved luminescence for high affinity antibody-ligand interaction thermodynamics and kinetics.

Aweda, Tolulope A / Meares, Claude F

Methods (San Diego, Calif.)

2011 Volume 56, Issue 2, Page(s) 145–153

Abstract: For experiments using synthetic ligands as probes for biological experiments, it is useful to determine the specificity and affinity of the ligands for their receptors. As ligands with higher affinities are developed (K(A)>10(8)M(-1); K(D)<10(-8)M), a ... ...

Abstract	For experiments using synthetic ligands as probes for biological experiments, it is useful to determine the specificity and affinity of the ligands for their receptors. As ligands with higher affinities are developed (K(A)>10(8)M(-1); K(D)<10(-8)M), a new challenge arises: to measure these values accurately. Isothermal titration calorimetry measures heat produced or consumed during ligand binding, and also provides the equilibrium binding constant. However, as normally practiced, its range is limited. Displacement titration, where a competing weaker ligand is used to lower the apparent affinity of the stronger ligand, can be used to determine the binding affinity as well as the complete thermodynamic data for ligand-antibody complexes with very high affinity. These equilibrium data have been combined with kinetic measurements to yield the rate constants as well. We describe this methodology, using as an example antibody 2D12.5, which captures yttrium S-2-(4-aminobenzyl)-1, 4, 7, 10-tetraazacyclododecanetetraacetate.
MeSH term(s)	Antibodies/chemistry ; Antibody Affinity ; Antigen-Antibody Complex/analysis ; Antigen-Antibody Complex/chemistry ; Calorimetry/instrumentation ; Calorimetry/methods ; Chelating Agents/chemistry ; Fluorescence ; Kinetics ; Ligands ; Luminescent Measurements/instrumentation ; Luminescent Measurements/methods ; Macromolecular Substances/analysis ; Macromolecular Substances/chemistry ; Organometallic Compounds/chemistry ; Sensitivity and Specificity ; Temperature ; Thermodynamics ; Time Factors
Chemical Substances	Antibodies ; Antigen-Antibody Complex ; Chelating Agents ; Ligands ; Macromolecular Substances ; Organometallic Compounds ; yttrium 2-(4-aminobenzyl)-1,4,7,10-tetraazacyclododecanetetraacetate
Language	English
Publishing date	2011-09-20
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1066584-5
ISSN	1095-9130 ; 1046-2023
ISSN (online)	1095-9130
ISSN	1046-2023
DOI	10.1016/j.ymeth.2011.09.011
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Article: Antibodies with infinite affinity: origins and applications.

Butlin, Nathaniel G / Meares, Claude F

Accounts of chemical research

2006 Volume 39, Issue 10, Page(s) 780–787

Abstract: Antibodies with infinite affinity were developed with the aim of improving targeted delivery of metal complexes to sites of disease. This is part of a series of chemical technology developments for biomedical imaging and therapy. Using a combination of ... ...

Abstract	Antibodies with infinite affinity were developed with the aim of improving targeted delivery of metal complexes to sites of disease. This is part of a series of chemical technology developments for biomedical imaging and therapy. Using a combination of genetics and chemical synthesis, it addresses challenges in developing proteins that specifically bind synthetic molecules and do not release them. The result is a set of reagents that promise to capture any of a large variety of metallic elements under physiological conditions and hold them for long periods of time.
MeSH term(s)	Animals ; Antibodies/chemistry ; Antibodies/genetics ; Chelating Agents/chemistry ; Humans ; Metals/chemistry ; Models, Molecular ; Mutation/genetics ; Neoplasms/immunology ; Neoplasms/radiotherapy
Chemical Substances	Antibodies ; Chelating Agents ; Metals
Language	English
Publishing date	2006-10
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	1483291-4
ISSN	1520-4898 ; 0001-4842
ISSN (online)	1520-4898
ISSN	0001-4842
DOI	10.1021/ar020275e
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Article: Combination of isothermal titration calorimetry and time-resolved luminescence for high affinity antibody–ligand interaction thermodynamics and kinetics

Aweda, Tolulope A / Meares, Claude F

Methods. 2012 Feb., v. 56, no. 2

2012

Abstract	For experiments using synthetic ligands as probes for biological experiments, it is useful to determine the specificity and affinity of the ligands for their receptors. As ligands with higher affinities are developed (KA>10⁸M⁻¹; KD<10–⁸M), a new challenge arises: to measure these values accurately. Isothermal titration calorimetry measures heat produced or consumed during ligand binding, and also provides the equilibrium binding constant. However, as normally practiced, its range is limited. Displacement titration, where a competing weaker ligand is used to lower the apparent affinity of the stronger ligand, can be used to determine the binding affinity as well as the complete thermodynamic data for ligand–antibody complexes with very high affinity. These equilibrium data have been combined with kinetic measurements to yield the rate constants as well. We describe this methodology, using as an example antibody 2D12.5, which captures yttrium S-2-(4-aminobenzyl)-1, 4, 7, 10-tetraazacyclododecanetetraacetate.
Keywords	antibodies ; binding capacity ; calorimetry ; heat ; ligands ; luminescence ; receptors ; titration ; yttrium
Language	English
Dates of publication	2012-02
Size	p. 145-153.
Publishing place	Elsevier Inc.
Document type	Article
ZDB-ID	1066584-5
ISSN	1095-9130 ; 1046-2023
ISSN (online)	1095-9130
ISSN	1046-2023
DOI	10.1016/j.ymeth.2011.09.011
Database	NAL-Catalogue (AGRICOLA)

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Article ; Online: Antibody with Infinite Affinity for In Vivo Tracking of Genetically Engineered Lymphocytes.

Krebs, Simone / Ahad, Afruja / Carter, Lukas M / Eyquem, Justin / Brand, Christian / Bell, Meghan / Ponomarev, Vladimir / Reiner, Thomas / Meares, Claude F / Gottschalk, Stephen / Sadelain, Michel / Larson, Steven M / Weber, Wolfgang A

Journal of nuclear medicine : official publication, Society of Nuclear Medicine

2018 Volume 59, Issue 12, Page(s) 1894–1900

Abstract: There remains an urgent need for the noninvasive tracking of transfused chimeric antigen receptor (CAR) T cells to determine their biodistribution, viability, expansion, and antitumor functionality. DOTA antibody reporter 1 (DAbR1) comprises a single- ... ...

Abstract	There remains an urgent need for the noninvasive tracking of transfused chimeric antigen receptor (CAR) T cells to determine their biodistribution, viability, expansion, and antitumor functionality. DOTA antibody reporter 1 (DAbR1) comprises a single-chain fragment of the antilanthanoid-DOTA antibody 2D12.5/G54C fused to the human CD4-transmembrane domain and binds irreversibly to lanthanoid (
MeSH term(s)	Animals ; Cell Line, Tumor ; Cell Tracking/methods ; Genes, Reporter ; Heterocyclic Compounds, 1-Ring ; Humans ; Immunoglobulin Fragments/genetics ; Immunoglobulin Fragments/metabolism ; Immunotherapy, Adoptive ; Lutetium ; Male ; Mice ; Mice, Inbred ICR ; Mice, Inbred NOD ; Mice, Knockout ; Mice, SCID ; Positron Emission Tomography Computed Tomography/methods ; Radiation Dosage ; Radioisotopes ; Radiopharmaceuticals/chemistry ; Radiopharmaceuticals/pharmacokinetics ; Receptors, Chimeric Antigen/genetics ; Receptors, Chimeric Antigen/metabolism ; Single Photon Emission Computed Tomography Computed Tomography/methods ; T-Lymphocytes/cytology ; T-Lymphocytes/immunology ; T-Lymphocytes/metabolism ; Tissue Distribution ; Xenograft Model Antitumor Assays ; Yttrium Radioisotopes
Chemical Substances	Heterocyclic Compounds, 1-Ring ; Immunoglobulin Fragments ; Radioisotopes ; Radiopharmaceuticals ; Receptors, Chimeric Antigen ; Yttrium Radioisotopes ; Yttrium-86 ; immunoglobulin Fv ; 1,4,7,10-tetraazacyclododecane- 1,4,7,10-tetraacetic acid (1HTE449DGZ) ; Lutetium (5H0DOZ21UJ) ; Lutetium-177 (BRH40Y9V1Q)
Language	English
Publishing date	2018-06-14
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	80272-4
ISSN	1535-5667 ; 0097-9058 ; 0161-5505 ; 0022-3123
ISSN (online)	1535-5667
ISSN	0097-9058 ; 0161-5505 ; 0022-3123
DOI	10.2967/jnumed.118.208041
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Zs.MO 328: Show issues

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Article: Proteolytic DNA for mapping protein-DNA interactions.

Schmidt, Brian D / Meares, Claude F

Biochemistry

2002 Volume 41, Issue 13, Page(s) 4186–4192

Abstract: We describe a technique to determine sites on proteins involved in protein-DNA interactions. DNA was synthesized via polymerase chain reaction (PCR) to produce four polynucleotide products with phosphorothioate nucleotides at the A, T, G, or C residues. ... ...

Abstract	We describe a technique to determine sites on proteins involved in protein-DNA interactions. DNA was synthesized via polymerase chain reaction (PCR) to produce four polynucleotide products with phosphorothioate nucleotides at the A, T, G, or C residues. Limited conjugation with the chemical protease FeBABE results in the surface of DNA being randomly labeled at the phosphorothioate sites with this protein-cleaving reagent. After formation of a protein-DNA complex, the proteolytic DNA can be activated to cleave the protein backbone at sites near the DNA. This technique was used to study the bacterial RNA polymerase/lacUV5 DNA open promoter complex, about which significant structural information is available. Cleavage sites on the two largest subunits of RNA polymerase, beta and beta', agree well with a recent model based on the crystal structure of the core enzyme alpha(2)betabeta' [Naryshkin, N., Revyakin, A., Kim, Y., Mekler, V., and Ebright, R. H. (2000) Cell 101, 601-611]. The cleavage site present on alpha supports previous studies regarding DNA binding regions of the alpha subunit. Cleavage sites identified throughout the sigma(70) subunit help to orient it with respect to the open promoter complex.
MeSH term(s)	Bacterial Proteins ; Binding Sites ; DNA/biosynthesis ; DNA/chemistry ; DNA/metabolism ; DNA-Binding Proteins/metabolism ; DNA-Directed RNA Polymerases/genetics ; Electrophoresis, Polyacrylamide Gel ; Enzyme-Linked Immunosorbent Assay ; Genetic Techniques ; Models, Biological ; Models, Molecular ; Polymerase Chain Reaction ; Promoter Regions, Genetic ; Protein Binding ; Temperature ; Transcription, Genetic
Chemical Substances	Bacterial Proteins ; DNA-Binding Proteins ; DNA (9007-49-2) ; DNA-Directed RNA Polymerases (EC 2.7.7.6)
Language	English
Publishing date	2002-03-04
Publishing country	United States
Document type	Journal Article ; Research Support, U.S. Gov't, P.H.S.
ZDB-ID	1108-3
ISSN	1520-4995 ; 0006-2960
ISSN (online)	1520-4995
ISSN	0006-2960
DOI	10.1021/bi015582r
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Article ; Online: The pharmacokinetics of Zr-89 labeled liposomes over extended periods in a murine tumor model.

Seo, Jai Woong / Mahakian, Lisa M / Tam, Sarah / Qin, Shengping / Ingham, Elizabeth S / Meares, Claude F / Ferrara, Katherine W

Nuclear medicine and biology

2015 Volume 42, Issue 2, Page(s) 155–163

Abstract: 89)Zr (t1/2=78.4h), a positron-emitting metal, has been exploited for PET studies of antibodies because of its relatively long decay time and facile labeling procedures. Here, we used (89)Zr to evaluate the pharmacokinetics of long-circulating liposomes ...

Abstract	(89)Zr (t1/2=78.4h), a positron-emitting metal, has been exploited for PET studies of antibodies because of its relatively long decay time and facile labeling procedures. Here, we used (89)Zr to evaluate the pharmacokinetics of long-circulating liposomes over 168h (1week). We first developed a liposomal-labeling method using p-isothiocyanatobenzyl-desferrioxamine (df-Bz-NCS) and df-PEG1k-DSPE. Df-Bz-NCS was conjugated to 1mol% amino- and amino-PEG2k-DSPE, where the 1mol% df-PEG1k-DSPE was incorporated when the liposomes were formulated. Incubation of (89)Zr with df, df-PEG1k, and df-PEG2k liposomes for one hour resulted in greater than 68% decay-corrected yield. The loss of the (89)Zr label from liposomes after incubation in 50% human serum for 48h ranged from ~1 to 3% across the three formulations. Tail vein administration of the three liposomal formulations in NDL tumor-bearing mice showed that the (89)Zr label at the end of the PEG2k brush was retained in the tumor, liver, spleen and whole body for a longer time interval than (89)Zr labels located under the PEG2k brush. The blood clearance rate of all three liposomal formulations was similar. Overall, the results indicate that the location of the (89)Zr label altered the clearance rate of intracellularly-trapped radioactivity and that df-PEG1k-DSPE provides a stable chelation site for liposomal or lipid-based particle studies over extended periods of time.
MeSH term(s)	Animals ; Chemistry, Pharmaceutical ; Deferoxamine/chemistry ; Disease Models, Animal ; Drug Stability ; Humans ; Isotope Labeling ; Liposomes/chemistry ; Liposomes/pharmacokinetics ; Mammary Neoplasms, Experimental/diagnostic imaging ; Mice ; Phosphatidylethanolamines/chemistry ; Polyethylene Glycols/chemistry ; Positron-Emission Tomography ; Radioisotopes ; Tissue Distribution ; Zirconium
Chemical Substances	Liposomes ; Phosphatidylethanolamines ; Radioisotopes ; 1,2-distearoylphosphatidylethanolamine (1G4B5265CQ) ; Polyethylene Glycols (30IQX730WE) ; Zirconium (C6V6S92N3C) ; Deferoxamine (J06Y7MXW4D)
Language	English
Publishing date	2015-02
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural
ZDB-ID	1138098-6
ISSN	1872-9614 ; 0883-2897 ; 0969-8051
ISSN (online)	1872-9614
ISSN	0883-2897 ; 0969-8051
DOI	10.1016/j.nucmedbio.2014.09.001
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Article: Irreversibly binding anti-metal chelate antibodies: Artificial receptors for pretargeting.

Corneillie, Todd M / Whetstone, Paul A / Meares, Claude F

Journal of inorganic biochemistry

2006 Volume 100, Issue 5-6, Page(s) 882–890

Abstract: Antibodies against metal chelates may potentially be used in biomedical applications such as targeted imaging and therapy of cancer. Highly specific monoclonal antibodies can be developed, but their binding strength needs to be maximized for them to be ... ...

Abstract	Antibodies against metal chelates may potentially be used in biomedical applications such as targeted imaging and therapy of cancer. Highly specific monoclonal antibodies can be developed, but their binding strength needs to be maximized for them to be of practical use. In general, the half-life for dissociation of an antibody-ligand complex is more than an order of magnitude lower than the half-lifetimes for decay of medically useful radiometal ions. Practically speaking, the metal chelate-based ligand will not be bound to its receptor long enough for all of the bound radiometal to decay. A novel approach to this problem is a combination of synthetic chemistry and site-directed mutagenesis, to position a mildly reactive group on the metal chelate adjacent to a complementary reactive group on the antibody when the complex is formed. The partners are chosen to be sufficiently unreactive so that they coexist with other molecules in living systems without undergoing reaction. When the antibody-chelate complex is formed the effective local concentrations of the two groups can be non-physically large, so that a permanent link is formed in the complex even though no reaction occurs when the partners are free in solution.
MeSH term(s)	Antibodies/genetics ; Antibodies/immunology ; Binding Sites, Antibody ; Chelating Agents ; Ligands ; Metals/immunology ; Mutagenesis, Site-Directed ; Receptors, Cell Surface/immunology
Chemical Substances	Antibodies ; Chelating Agents ; Ligands ; Metals ; Receptors, Cell Surface
Language	English
Publishing date	2006-05
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Review
ZDB-ID	162843-4
ISSN	1873-3344 ; 0162-0134
ISSN (online)	1873-3344
ISSN	0162-0134
DOI	10.1016/j.jinorgbio.2006.01.004
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