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Related Concept Videos

Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...

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Related Experiment Video

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Quantification of Proteins Using Peptide Immunoaffinity Enrichment Coupled with Mass Spectrometry
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Quantification of Proteins Using Peptide Immunoaffinity Enrichment Coupled with Mass Spectrometry

Published on: July 31, 2011

Quantitative serum proteomics from surface plasmon resonance imaging.

Christopher Lausted1, Zhiyuan Hu, Leroy Hood

  • 1Institute for Systems Biology, Seattle, Washington 98103, USA. clausted@systemsbiology.org

Molecular & Cellular Proteomics : MCP
|August 6, 2008
PubMed
Summary
This summary is machine-generated.

This study introduces a fast, label-free method using surface plasmon resonance imaging of antibody microarrays for protein analysis in serum. The technique enables accurate quantification and distinguishes disease-specific protein profiles, aiding biomarker discovery.

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Area of Science:

  • Proteomics
  • Biomarker Discovery
  • Analytical Chemistry

Background:

  • Accurate protein detection and quantification in complex biological samples like serum are crucial for advancing proteomics and developing disease biomarkers.
  • Existing methods often face challenges in speed, efficiency, and multiparameter profiling capabilities.

Purpose of the Study:

  • To establish a high-throughput, label-free method for serum protein analysis using surface plasmon resonance imaging (SPRI) of antibody microarrays.
  • To validate the system for absolute and relative protein quantification and demonstrate its utility in distinguishing disease-related protein profiles.

Main Methods:

  • Fabrication of antibody microarrays on gold substrates via standard pin spotting.
  • Serum sample analysis using a camera-based surface plasmon resonance system for label-free binding detection.
  • Validation using known protein concentrations (transferrin, albumin) and comparison with ELISA; application to compare serum profiles of liver cancer patients versus controls.

Main Results:

  • Accurate quantification of transferrin and albumin in human and murine serum, closely matching ELISA results.
  • Achieved lower limits of detection ranging from 14 to 58 ng/ml (175 to 755 pM).
  • Successfully differentiated serum protein profiles between liver cancer patients and healthy controls, identifying 39 significant protein changes, including elevated alpha-Fetoprotein.

Conclusions:

  • The developed SPRI antibody microarray system offers a feasible, high-throughput approach for both absolute and relative protein quantification in serum.
  • This method holds significant potential for accelerating biomarker discovery and disease profiling in proteomics.
  • The ability to distinguish disease-specific profiles highlights the system's utility in clinical diagnostics and research.