Advanced

Protein chips based on recombinant antibody fragments: A highly sensitive approach as detected by mass spectrometry

Borrebaeck, Carl LU ; Ekstrom, S.; Hager, A. C. M.; Nilsson, J.; Laurell, Thomas LU and Marko-Varga, György LU (2001) In BioTechniques 30(5). p.1126-1126
Abstract
With the human genome in a first sequence draft and several other genomes being finished this year, the existing information gap between genomics and proteomics is becoming increasingly evident. The analysis of the proteome is, however, much more complicated because the synthesis and structural requirements of functional proteins are different from the easily handled oligonucleotides for which a first analytical breakthrough already has come in the use of DNA chips. In comparison with the DNA microarrays, the protein arrays, or protein chips, offer the distinct possibility of developing a rapid global analysis of the entire proteome. Thus, the concept of comparing proteomic maps of healthy and diseased cells may allow us to understand cell... (More)
With the human genome in a first sequence draft and several other genomes being finished this year, the existing information gap between genomics and proteomics is becoming increasingly evident. The analysis of the proteome is, however, much more complicated because the synthesis and structural requirements of functional proteins are different from the easily handled oligonucleotides for which a first analytical breakthrough already has come in the use of DNA chips. In comparison with the DNA microarrays, the protein arrays, or protein chips, offer the distinct possibility of developing a rapid global analysis of the entire proteome. Thus, the concept of comparing proteomic maps of healthy and diseased cells may allow us to understand cell signaling and metabolic pathways and will form a novel base for pharmaceutical companies to develop future therapeutics much more rapidly. This report demonstrates the possibilities of designing protein chips based on specially constructed, small recombinant antibody fragments using nanostructure surfaces with biocompatible characteristics, resulting in sensitive detection in the 600-amol range. The assay readout allows the determination of single or multiple antigen-antibody interactions. Mass identity of the antigens, currently with a resolution of 8000, enables the detection of structural modifications of single proteins. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
BioTechniques
volume
30
issue
5
pages
1126 - 1126
publisher
Informa Healthcare
external identifiers
  • wos:000168636500035
  • scopus:0035003057
ISSN
0736-6205
language
English
LU publication?
yes
id
727677ea-f62c-49da-b7ce-941f552cf085 (old id 2376267)
date added to LUP
2012-03-23 09:51:48
date last changed
2018-01-07 09:23:07
@article{727677ea-f62c-49da-b7ce-941f552cf085,
  abstract     = {With the human genome in a first sequence draft and several other genomes being finished this year, the existing information gap between genomics and proteomics is becoming increasingly evident. The analysis of the proteome is, however, much more complicated because the synthesis and structural requirements of functional proteins are different from the easily handled oligonucleotides for which a first analytical breakthrough already has come in the use of DNA chips. In comparison with the DNA microarrays, the protein arrays, or protein chips, offer the distinct possibility of developing a rapid global analysis of the entire proteome. Thus, the concept of comparing proteomic maps of healthy and diseased cells may allow us to understand cell signaling and metabolic pathways and will form a novel base for pharmaceutical companies to develop future therapeutics much more rapidly. This report demonstrates the possibilities of designing protein chips based on specially constructed, small recombinant antibody fragments using nanostructure surfaces with biocompatible characteristics, resulting in sensitive detection in the 600-amol range. The assay readout allows the determination of single or multiple antigen-antibody interactions. Mass identity of the antigens, currently with a resolution of 8000, enables the detection of structural modifications of single proteins.},
  author       = {Borrebaeck, Carl and Ekstrom, S. and Hager, A. C. M. and Nilsson, J. and Laurell, Thomas and Marko-Varga, György},
  issn         = {0736-6205},
  language     = {eng},
  number       = {5},
  pages        = {1126--1126},
  publisher    = {Informa Healthcare},
  series       = {BioTechniques},
  title        = {Protein chips based on recombinant antibody fragments: A highly sensitive approach as detected by mass spectrometry},
  volume       = {30},
  year         = {2001},
}