LrgpV1, Istex, Corpus, bibRecord, 000704

Two‐Dimensional 1H‐nmr study of antigen–antibody interactions: Binding of synthetic decapeptides to an anti‐acetylcholine receptor monoclonal antibody

Identifieur interne : 000704 ( Istex/Corpus ); précédent : 000703; suivant : 000705

Two‐Dimensional 1H‐nmr study of antigen–antibody interactions: Binding of synthetic decapeptides to an anti‐acetylcholine receptor monoclonal antibody

Auteurs : Manh Thong Cung ; Pascal Demange ; Michel Marraud ; Vassilios Tsikaris ; Constantinos Sakarellos ; Irene Papadouli ; Anna Kokla ; Socrates J. Tzartos

Source :

Biopolymers [ 0006-3525 ] ; 1991-05.

RBID : ISTEX:21D51F31B1D42F3EA459A7A8E59DB4A784674932

English descriptors

Abstract

Two‐dimensional NMR experiments [correlated spectroscopy (COSY) and two‐dimensional transferred nuclear Overhauser enhancement spectroscopy (TR‐NOESY)] have been applied to study the interactions of a monoclonal antibody (mAb) directed to the main immunogenic region (MIR) of the acetylcholine receptor (AChR), and four synthetic decapeptides from the MIR. The decapeptides were the Torpedo AChR α67‐76 fragment (W 67‐N68‐P69‐A70‐D71‐Y72‐G73‐G74‐I75‐K76) and its three [A69], [A73], and [A76] analogues. The results led to the following conclusions: (1) the magnitude of the TR‐NOE cross peaks does not depend only on the structuration of the peptide in the bound state, but also on restrictions of the mobility, i.e., on the correlation time τc, which can be different for every residue; (2) the binding capacity of the synthetic peptides to mAbs measured by radioimmunoassay is directly correlated to the NOE magnitude; and (3) the combined interpretation of the COSY and TR‐NOESY experiments gives a qualitative information about the nature and the overall conformation of the sequence which is in contact with the mAb binding site.

Url:

https://api.istex.fr/document/21D51F31B1D42F3EA459A7A8E59DB4A784674932/fulltext/pdf

DOI: 10.1002/bip.360310622

Links to Exploration step

ISTEX:21D51F31B1D42F3EA459A7A8E59DB4A784674932

Le document en format XML

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<front><div type="abstract" xml:lang="en">Two‐dimensional NMR experiments [correlated spectroscopy (COSY) and two‐dimensional transferred nuclear Overhauser enhancement spectroscopy (TR‐NOESY)] have been applied to study the interactions of a monoclonal antibody (mAb) directed to the main immunogenic region (MIR) of the acetylcholine receptor (AChR), and four synthetic decapeptides from the MIR. The decapeptides were the Torpedo AChR α67‐76 fragment (W 67‐N68‐P69‐A70‐D71‐Y72‐G73‐G74‐I75‐K76) and its three [A69], [A73], and [A76] analogues. The results led to the following conclusions: (1) the magnitude of the TR‐NOE cross peaks does not depend only on the structuration of the peptide in the bound state, but also on restrictions of the mobility, i.e., on the correlation time τc, which can be different for every residue; (2) the binding capacity of the synthetic peptides to mAbs measured by radioimmunoassay is directly correlated to the NOE magnitude; and (3) the combined interpretation of the COSY and TR‐NOESY experiments gives a qualitative information about the nature and the overall conformation of the sequence which is in contact with the mAb binding site.</div>
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H‐nmr study of antigen–antibody interactions: Binding of synthetic decapeptides to an anti‐acetylcholine receptor monoclonal antibody</title>
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Two‐Dimensional 1H‐nmr study of antigen–antibody interactions: Binding of synthetic decapeptides to an anti‐acetylcholine receptor monoclonal antibody

Two‐Dimensional 1H‐nmr study of antigen–antibody interactions: Binding of synthetic decapeptides to an anti‐acetylcholine receptor monoclonal antibody

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