Electrospray Ionization–Ion Mobility Spectrometry Identified Monoclonal Antibodies that Bind Exclusively to Either the Monomeric or a Dimeric Form of Prostate Specific Antigen

doi:10.1021/ac301527v

Title: Electrospray Ionization–Ion Mobility Spectrometry Identified Monoclonal Antibodies that Bind Exclusively to Either the Monomeric or a Dimeric Form of Prostate Specific Antigen

Full Record
Other Related Research

Authors:

Blake, II, Robert C. ^[1]; Blake, Diane A. ^[2]

Division of Basic Pharmaceutical Sciences, College of Pharmacy, Xavier University of Louisiana, New Orleans, Louisiana 70125, United States
Department of Biochemistry and Molecular Biology, Tulane University School of Medicine, New Orleans, Louisiana 70112, United States

Publication Date:: 2012-07-12

Sponsoring Org.:: USDOE

OSTI Identifier:: 1123368

Resource Type:: Published Article

Journal Name:: Analytical Chemistry

Additional Journal Information:: Journal Name: Analytical Chemistry Journal Volume: 84 Journal Issue: 15; Journal ID: ISSN 0003-2700

Publisher:: American Chemical Society

Country of Publication:: United States

Language:: English

Citation Formats


                    Blake, II, Robert C., and Blake, Diane A. Electrospray Ionization–Ion Mobility Spectrometry Identified Monoclonal Antibodies that Bind Exclusively to Either the Monomeric or a Dimeric Form of Prostate Specific Antigen.  United States: N. p., 2012. 
        Web.  doi:10.1021/ac301527v.

Copy to clipboard


                    Blake, II, Robert C., & Blake, Diane A. Electrospray Ionization–Ion Mobility Spectrometry Identified Monoclonal Antibodies that Bind Exclusively to Either the Monomeric or a Dimeric Form of Prostate Specific Antigen.  United States.  doi:10.1021/ac301527v.

Copy to clipboard


                    Blake, II, Robert C., and Blake, Diane A. Thu .  
        "Electrospray Ionization–Ion Mobility Spectrometry Identified Monoclonal Antibodies that Bind Exclusively to Either the Monomeric or a Dimeric Form of Prostate Specific Antigen".  United States.  doi:10.1021/ac301527v.

Copy to clipboard


                    
@article{osti_1123368,

  title        = {Electrospray Ionization–Ion Mobility Spectrometry Identified Monoclonal Antibodies that Bind Exclusively to Either the Monomeric or a Dimeric Form of Prostate Specific Antigen},

  author       = {Blake, II, Robert C. and Blake, Diane A.},

  abstractNote = {},

  doi          = {10.1021/ac301527v},

  journal      = {Analytical Chemistry},

  number       = 15,

  volume       = 84,

  place        = {United States},

  year         = {2012},

  month        = {7}

}

Copy to clipboard

Journal Article:

Free Publicly Available Full Text

Publisher's Version of Record
DOI: 10.1021/ac301527v

Other availability

Search WorldCat to find libraries that may hold this journal

Save / Share:

Export Metadata

Save to My Library

Similar Records in DOE PAGES and OSTI.GOV collections:

Native Mass Spectrometry, Ion mobility, and Collision-Induced Unfolding Categorize Malaria Antigen/Antibody Binding

Journal Article Huang, Yining ; Salinas, Nichole D. ; Chen, Edwin ; ... - Journal of the American Society for Mass Spectrometry

Plasmodium vivax Duffy Binding Protein (PvDBP) is a promising vaccine candidate for P. vivax malaria. Recently, we reported the epitopes on PvDBP region II (PvDBP-II) for three inhibitory monoclonal antibodies (2D10, 2H2, and 2C6). In this communication, we describe the combination of native mass spectrometry and ion mobility (IM) with collision induced unfolding (CIU) to study the conformation and stabilities of three malarial antigen–antibody complexes. These complexes, when collisionally activated, undergo conformational changes that depend on the location of the epitope. CIU patterns for PvDBP-II in complex with antibody 2D10 and 2H2 are highly similar, indicating comparable binding topology andmore »« less
DOI: 10.1007/S13361-017-1782-0
Crystal structure of the antigen-binding fragment of a monoclonal antibody specific for the multidrug-resistance-linked ABC transporter human P-glycoprotein

Journal Article Esser, Lothar ; Shukla, Suneet ; Zhou, Fei ; ... - Acta Crystallographica. Section F, Structural Biology Communications

P-glycoprotein (P-gp) is a polyspecific ATP-dependent transporter linked to multidrug resistance in cancers that plays important roles in the pharmacokinetics of a large number of drugs. The drug-resistance phenotype of P-gp can be modulated by the monoclonal antibody UIC2, which specifically recognizes human P-gp in a conformation-dependent manner. Here, the purification, sequence determination and high-resolution structure of the Fab fragment of UIC2 (UIC2/Fab) are reported. Purified UIC2/Fab binds human P-gp with a 1:1 stoichiometry. Crystals of UIC2/Fab are triclinic (space groupP1), with unit-cell parametersa= 40.67,b= 44.91,c= 58.09 Å, α = 97.62, β = 99.10, γ = 94.09°, and diffracted X-rays tomore »« less
DOI: 10.1107/S2053230X16009778
A Remote Arene-Binding Site on Prostate Specific Membrane Antigen Revealed by Antibody-Recruiting Small Molecules

Journal Article Zhang, Andrew X ; Murelli, Ryan P ; Barinka, Cyril ; ... - J. Am. Chem. Soc.

Prostate specific membrane antigen (PSMA) is a membrane-bound glutamate carboxypeptidase overexpressed in many forms of prostate cancer. Our laboratory has recently disclosed a class of small molecules, called ARM-Ps (antibody-recruiting molecule targeting prostate cancer) that are capable of enhancing antibody-mediated immune recognition of prostate cancer cells. Interestingly, during the course of these studies, we found ARM-Ps to exhibit extraordinarily high potencies toward PSMA, compared to previously reported inhibitors. Here, we report in-depth biochemical, crystallographic, and computational investigations which elucidate the origin of the observed affinity enhancement. These studies reveal a previously unreported arene-binding site on PSMA, which we believe participatesmore »« less
DOI: 10.1021/ja104591m
Rapid assessment of human amylin aggregation and its inhibition by copper(II) ions by laser ablation electrospray ionization mass spectrometry with ion mobility separation

Journal Article Li, Hang ; Ha, Emmeline ; Donaldson, Robert P. ; ... - Analytical Chemistry

Native electrospray ionization (ESI) mass spectrometry (MS) is often used to monitor noncovalent complex formation between peptides and ligands. The relatively low throughput of this technique, however, is not compatible with extensive screening. Laser ablation electrospray ionization (LAESI) MS combined with ion mobility separation (IMS) can analyze complex formation and provide conformation information within a matter of seconds. Islet amyloid polypeptide (IAPP) or amylin, a 37-amino acid residue peptide, is produced in pancreatic beta-cells through proteolytic cleavage of its prohormone. Both amylin and its precursor can aggregate and produce toxic oligomers and fibrils leading to cell death in the pancreasmore »« less
Cited by 7
DOI: 10.1021/acs.analchem.5b02217

Full Text Available
Laser-ablation electrospray ionization mass spectrometry with ion mobility separation reveals metabolites in the symbiotic interactions of soybean roots and rhizobia

Journal Article Stopka, Sylwia A. ; Agtuca, Beverly J. ; Koppenaal, David W. ; ... - The Plant Journal

Technologies enabling in situ metabolic profiling of living plant systems are invaluable for understanding physiological processes and could be used for rapid phenotypic screening (e.g., to produce plants with superior biological nitrogen fixing ability). The symbiotic interaction between legumes and nitrogen-fixing soil bacteria results in a specialized plant organ (i.e., root nodule), where the exchange of nutrients between host and endosymbiont occurs. Laser ablation electrospray ionization mass spectrometry (LAESI-MS) is a method that can be performed under ambient conditions requiring minimal sample preparation. Here, we employed LAESI-MS to explore the well-characterized symbiosis between soybean (Glycine max L. Merr.) and itsmore »« less
DOI: 10.1111/tpj.13569

Similar Records