Affinity capture mass spectrometry of biomarker proteins using peptide ligands from biopanning

Erin M. Johnson, Walther R. Ellis, Linda S. Powers, Vicki H. Wysocki

Research output: Contribution to journalArticle

8 Scopus citations


Affinity capture mass spectrometry was used to isolate and ionize protein A from Staphylococcus aureusfrom both a commercial source and cell culture lysate using matrix assisted laser desorption/ionization (MALDI) mass spectrometry. Two surfaces are compared: gold surfaces with immunoglobulin G covalently immobilized and silica surfaces with a covalently bound small peptide discovered via biopanning. A detection limit of 2.22 bacterial cells/mL of culture fluid was determined for the immobilized peptide surfaces. This study emphasizes the ability to use peptide ligands to effectively capture a biomarker protein out of a complex mixture. This demonstrates the potential to use biopanning to generate capture ligands for a large variety of target proteins and subsequently detect the captured protein using MALDI mass spectrometry.

Original languageEnglish (US)
Pages (from-to)5999-6005
Number of pages7
JournalAnalytical chemistry
Issue number15
StatePublished - Aug 1 2009


ASJC Scopus subject areas

  • Analytical Chemistry

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