Polymeric Inverse Micelles as Selective Peptide Extraction Agents for MALDI-MS Analysis

Analyses of peptides in complex mixtures are significant challenges in proteomics applications. Here, we report an amphiphilic polymer-based nanoassembly that is capable of selectively extracting peptides, on the basis of their isoelectric points, into an immiscible organic phase from an aqueous sol...

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Bibliographic Details
Published in:Analytical chemistry (Washington) 2007-09, Vol.79 (18), p.7124-7130
Main Authors: Combariza, Marianny Y, Savariar, Elamprakash N, Vutukuri, Dharma Rao, Thayumanavan, S, Vachet, Richard W
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Analytical chemistry
Animals
Aqueous chemistry
Aqueous solutions
Biochemistry
Chemistry
Exact sciences and technology
Hydrogen-Ion Concentration
Isoelectric Point
Micelles
Molecular Sequence Data
Molecular Structure
Myoglobin - analysis
Myoglobin - chemistry
Organic Chemicals - chemistry
Peptides
Peptides - analysis
Peptides - chemistry
Polymers - chemistry
Proteomics
Sensitivity and Specificity
Spectrometric and optical methods
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Water - chemistry
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Summary:Analyses of peptides in complex mixtures are significant challenges in proteomics applications. Here, we report an amphiphilic polymer-based nanoassembly that is capable of selectively extracting peptides, on the basis of their isoelectric points, into an immiscible organic phase from an aqueous solution. The isoelectric point (pI) cutoff in these extractions depends on the pH of the aqueous solution, and thus, sequential fractionation of peptide mixtures based on pI can be accomplished by varying the pH of the aqueous solution. Additionally, we observe an unexpected enhancement in the MALDI-MS signal for extracted peptides ionized in the presence of the polymer, which allows us to obtain reproducible ion signals for some peptides at concentrations as low as 10 pM.
ISSN:0003-2700
1520-6882
DOI:10.1021/ac071001d