Document Detail

Epitope-specificity of recombinant antibodies reveals promiscuous peptide-binding properties.
MedLine Citation:
PMID:  23034898     Owner:  NLM     Status:  MEDLINE    
Protein-peptide interactions are a common occurrence and essential for numerous cellular processes, and frequently explored in broad applications within biology, medicine, and proteomics. Therefore, understanding the molecular mechanism(s) of protein-peptide recognition, specificity, and binding interactions will be essential. In this study, we report the first detailed analysis of antibody-peptide interaction characteristics, by combining large-scale experimental peptide binding data with the structural analysis of eight human recombinant antibodies and numerous peptides, targeting tryptic mammalian and eukaryote proteomes. The results consistently revealed that promiscuous peptide-binding interactions, that is, both specific and degenerate binding, were exhibited by all antibodies, and the discovery was corroborated by orthogonal data, indicating that this might be a general phenomenon for low-affinity antibody-peptide interactions. The molecular mechanism for the degenerate peptide-binding specificity appeared to be executed through the use of 2-3 semi-conserved anchor residues in the C-terminal part of the peptides, in analogue to the mechanism utilized by the major histocompatibility complex-peptide complexes. In the long-term, this knowledge will be instrumental for advancing our fundamental understanding of protein-peptide interactions, as well as for designing, generating, and applying peptide specific antibodies, or peptide-binding proteins in general, in various biotechnical and medical applications.
Niclas Olsson; Stefan Wallin; Peter James; Carl A K Borrebaeck; Christer Wingren
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't     Date:  2012-10-25
Journal Detail:
Title:  Protein science : a publication of the Protein Society     Volume:  21     ISSN:  1469-896X     ISO Abbreviation:  Protein Sci.     Publication Date:  2012 Dec 
Date Detail:
Created Date:  2012-11-27     Completed Date:  2013-04-29     Revised Date:  2013-12-04    
Medline Journal Info:
Nlm Unique ID:  9211750     Medline TA:  Protein Sci     Country:  United States    
Other Details:
Languages:  eng     Pagination:  1897-910     Citation Subset:  IM    
Copyright Information:
Copyright © 2012 The Protein Society.
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MeSH Terms
Amino Acid Sequence
Antibody Specificity
Epitopes / chemistry,  immunology*
Mass Spectrometry
Models, Molecular
Molecular Sequence Data
Peptides / chemistry*,  immunology*
Protein Conformation
Recombinant Proteins / chemistry,  immunology
Single-Chain Antibodies / chemistry*,  immunology*
Reg. No./Substance:
0/Epitopes; 0/Peptides; 0/Recombinant Proteins; 0/Single-Chain Antibodies

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