Antibody Recognition of Chiral Surfaces. Enantiomorphous Crystals of Leucine-Leucine-Tyrosine

Monoclonal antibodies were selected after immunization with crystals of the tripeptide l-leucine-l-leucine-l-tyrosine. They interact with the tripeptide crystals, but do not interact with the tripeptide molecule, with other crystalline surfaces, or with adsorbed protein. The interactions of two anti...

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Bibliographic Details
Published in:Journal of the American Chemical Society 2003-01, Vol.125 (3), p.696-704
Main Authors: Geva, Merav, Frolow, Felix, Eisenstein, Miriam, Addadi, Lia
Format: Article
Language:English
Subjects:
Adjuvants, Immunologic - chemistry
Animals
Antibodies, Monoclonal - chemistry
Antibodies, Monoclonal - immunology
Antibody Formation
Antibody Specificity
Biological and medical sciences
Crystallization
Crystallography, X-Ray
Female
Fundamental and applied biological sciences. Psychology
Immunization
Interactions. Associations
Intermolecular phenomena
Mice
Mice, Inbred BALB C
Models, Molecular
Molecular biophysics
Oligopeptides - chemistry
Oligopeptides - immunology
Protein Conformation
Stereoisomerism
Surface Properties
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Summary:Monoclonal antibodies were selected after immunization with crystals of the tripeptide l-leucine-l-leucine-l-tyrosine. They interact with the tripeptide crystals, but do not interact with the tripeptide molecule, with other crystalline surfaces, or with adsorbed protein. The interactions of two antibodies with crystals of l-Leu-l-Leu-l-Tyr and of its enantiomer d-Leu-d-Leu-d-Tyr were characterized in depth. Antibody 48E is stereoselective and enantioselective:  it recognizes only the {01̄1} faces of the l-Leu-l-Leu-l-Tyr crystals, and not the enantiomorphous {011̄} faces of d-Leu-d-Leu-d-Tyr crystals, or any other faces of either crystal. In contrast, antibody 602E is poorly stereoselective and is not enantioselective:  it recognizes the crystals of both enantiomers, interacting with a number of different faces of each. The different recognition patterns are explained on the basis of the nature of the interactions and the structure of the interacting surfaces. Understanding this antibody specificity advances our general understanding of surface recognition and transfer of chiral information across biological interfaces.
ISSN:0002-7863
1520-5126
DOI:10.1021/ja027942j