[NMR paper] Expression and structural characterization of anti-T-antigen single chain antibodies (scFvs) and analysis of their binding to T-antigen by surface plasmon resonance and NMR spectroscopy.
Expression and structural characterization of anti-T-antigen single chain antibodies (scFvs) and analysis of their binding to T-antigen by surface plasmon resonance and NMR spectroscopy.
Expression and structural characterization of anti-T-antigen single chain antibodies (scFvs) and analysis of their binding to T-antigen by surface plasmon resonance and NMR spectroscopy.
J Biochem. 2013 Oct 4;
Authors: Yuasa N, Koyama T, Subedi GP, Yamaguchi Y, Matsushita M, Fujita-Yamaguchi Y
Abstract
T-antigen (Gal?1-3GalNAc?-1-Ser/Thr), also known as Thomsen-Friendenreich antigen (TF antigen), is an oncofetal antigen commonly found in cancerous tissues. Availability of anti-T-antigen human antibodies could lead to the development of cancer diagnostics and therapeutics. Four groups of single-chain variable fragment (scFv) genes were previously isolated from a phage library (Matsumoto-Takasaki et al. BioScience Trends 3, 87-95). Here, four anti-T-antigen scFv genes belonging to Group 1-4 were expressed and produced in a Drosophila S2 cell expression system. ELISA and SPR analyses confirmed the binding activity of 1E8 scFv protein to various T-antigen presenting conjugates. NMR experiments provided evidence of the folded nature of the 1E8 scFv protein. ScFv-ligand contact was identified by STD NMR, indicating that the galactose unit of T-antigen at the non-reducing end was primarily recognized by 1E8 scFv. This thus provides direct evidence of T-antigen specificity.
PMID: 24098012 [PubMed - as supplied by publisher]
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain
March 2012
Publication year: 2012
Source:Biochimie, Volume 94, Issue 3</br>
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The insulin-like growth factor binding proteins are a family of six proteins (IGFBP-1 to -6) that bind insulin-like growth factors-I and -II (IGF-I/II) with high affinity. In addition to regulating IGF actions, IGFBPs have IGF-independent functions. IGFBP-2, the largest member of this family, is over-expressed in many cancers and has been proposed as a possible target for the...
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Biochimie. 2011 Sep 22;
Authors: Galea CA, Mobli M, McNeil KA, Mulhern TD, Wallace JC, King GF, Forbes BE, Norton RS
Abstract
The insulin-like growth factor binding proteins are a family of six proteins (IGFBP-1 to 6) that bind insulin-like growth factors-I and -II (IGF-I/II) with high affinity. In addition...
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09-30-2011 06:00 AM
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Insulin-like growth factor binding protein-2: NMR analysis and structural characterization of the N-terminal domain.
Biochimie. 2011 Sep 22;
Authors: Galea CA, Mobli M, McNeil KA, Mulhern TD, Wallace JC, King GF, Forbes BE, Norton RS
Abstract
The insulin-like growth factor binding proteins are a family of six proteins (IGFBP-1 to 6) that bind insulin-like growth factors-I and -II (IGF-I/II) with high affinity. In...
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09-30-2011 05:59 AM
[NMR paper] NMR study on the interaction between MHC class I protein and its antigen peptide.
NMR study on the interaction between MHC class I protein and its antigen peptide.
Related Articles NMR study on the interaction between MHC class I protein and its antigen peptide.
Biochem Biophys Res Commun. 2000 Nov 30;278(3):609-13
Authors: Nakagawa M, Chiba-Kamoshida K, Udaka K, Nakanishi H
A major histcompatibility complex (MHC) class I protein H-2K(b) was expressed in a large scale as a fusion protein with thioredoxin and hexahistidine at the N-terminus to analyze the interaction with the antigen peptide SIYRYYGL. NMR spectra of the...
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11-19-2010 08:29 PM
[NMR paper] NMR identification of epitopes of Lyme disease antigen OspA to monoclonal antibodies.
NMR identification of epitopes of Lyme disease antigen OspA to monoclonal antibodies.
Related Articles NMR identification of epitopes of Lyme disease antigen OspA to monoclonal antibodies.
J Mol Biol. 1998 Aug 7;281(1):61-7
Authors: Huang X, Yang X, Luft BJ, Koide S
Outer surface protein A (OspA) from the Lyme disease spirochete Borrelia burgdorferi has been a focus of vaccine development. We have identified epitopes of OspA to two monoclonal antibodies (mAbs) by comparing NMR chemical shifts of free OspA and those in Fab complexes....
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11-17-2010 11:15 PM
[NMR paper] Identification of the single-stranded DNA binding surface of the transcriptional coac
Identification of the single-stranded DNA binding surface of the transcriptional coactivator PC4 by NMR.
http://www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-standard-jbc_full_free.gif Related Articles Identification of the single-stranded DNA binding surface of the transcriptional coactivator PC4 by NMR.
J Biol Chem. 1999 Feb 5;274(6):3693-9
Authors: Werten S, Wechselberger R, Boelens R, van der Vliet PC, Kaptein R
The C-terminal domain of the eukaryotic transcriptional cofactor PC4...
Expression and structural characterization of anti-T-antigen single chain antibodies (scFvs) and analysis of their binding to T-antigen by surface plasmon resonance and NMR spectroscopy.
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