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

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

Standard

Protein chips based on recombinant antibody fragments: A highly sensitive approach as detected by mass spectrometry. / Borrebaeck, Carl; Ekstrom, S.; Hager, A. C. M.; Nilsson, J.; Laurell, Thomas; Marko-Varga, György.

I: BioTechniques, Vol. 30, Nr. 5, 2001, s. 1126.

Forskningsoutput: TidskriftsbidragArtikel i vetenskaplig tidskrift

Harvard

APA

CBE

MLA

Vancouver

Author

RIS

TY - JOUR

T1 - Protein chips based on recombinant antibody fragments: A highly sensitive approach as detected by mass spectrometry

AU - Borrebaeck, Carl

AU - Ekstrom, S.

AU - Hager, A. C. M.

AU - Nilsson, J.

AU - Laurell, Thomas

AU - Marko-Varga, György

N1 - The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Analytical Chemistry (S/LTH) (011001004), Department of Immunotechnology (011029300), Biomedical Engineering (011200011)

PY - 2001

Y1 - 2001

N2 - 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.

AB - 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.

M3 - Article

VL - 30

SP - 1126

JO - BioTechniques

T2 - BioTechniques

JF - BioTechniques

SN - 0736-6205

IS - 5

ER -