Two-dimensional 1H-NMR study of antigen-antibody interactions: binding of synthetic decapeptides to an anti-acetylcholine receptor monoclonal antibody.

Title:

Two-dimensional 1H-NMR study of antigen-antibody interactions: binding of synthetic decapeptides to an anti-acetylcholine receptor monoclonal antibody.

Dataset

identifier:	1699777
description:	epitope description:WNPADYGGIK antigen name:Acetylcholine receptor subunit alpha host organism:Rattus norvegicus Lewis antibody name:mAb6
aggregation:	instance of dataset
availability:	available
primaryPublications:	1932573

Access

authorizations:	registration not required
accessURL:	http://www.iedb.org/reference/1010158
landingPage:	http://www.iedb.org/assay/1699777

Publication

type:	Literature
publicationVenue:	Biopolymers
dates:	1991

Dimension

study type:	b cell assays
subject species:	Tetronarce californica

Person

fullName:	M T Cung P Demange M Marraud V Tsikaris C Sakarellos I Papadouli A Kokla S J Tzartos

Data Type

method:	nuclear magnetic resonance (NMR)

Study

name:	Two-dimensional 1H-NMR study of antigen-antibody interactions: binding of synthetic decapeptides to an anti-acetylcholine receptor monoclonal antibody.
description:	The complex between the epitope and mAb6 directed to the main immunogenic region (MIR) of the AChR was analyzed by two-dimensional nmr. The results indicate that N-terminal residues WNPADY are in close contact with mAb6. In particular, Pro at position 3 interacts tightly with mAb6. The alanine-substituted analog peptides WNAADYGGIK (A69 analog), WNPADYAGIK (A73 analog), and WNPADYGGIA (A76 analog) bound to mAb6 with different affinities. Peptide A69 analog has a lower affinity while A73 and A76 analogs have about a 2-fold higher affinity. Residues in the C-terminal part of A76 analog interact with mAb6, unlike the epitope.

Data Repository

name:	iedb
homePage:	http://www.iedb.org

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