Detail publikace

Microfluidic Superheating for Peptide Sequence Elucidation

ALTMAYER, M. MANZ, A. NEUŽIL, P.

Originální název

Microfluidic Superheating for Peptide Sequence Elucidation

Anglický název

Microfluidic Superheating for Peptide Sequence Elucidation

Jazyk

en

Originální abstrakt

Herein, we introduce microfluidic superheating as a new method for peptide fragmentation prior to mass spectrometric analysis. The superheating conditions were found to be stable up to 240 C for more than 30 min without elevated pressure or boiling of the aqueous sample. As proof of principle, we exposed the peptides ACTH1-10 and OVA257-264 to various superheating conditions, causing different degrees of decomposition. Optimized superheating conditions resulted in the entire peptide ladder sequence of the y-ions, allowing the amino acid sequence to be deduced from a single-stage mass spectrum. Thus, obtaining information in the same quality as from tandem mass spectrometry can be achieved by a single superheating step.

Anglický abstrakt

Herein, we introduce microfluidic superheating as a new method for peptide fragmentation prior to mass spectrometric analysis. The superheating conditions were found to be stable up to 240 C for more than 30 min without elevated pressure or boiling of the aqueous sample. As proof of principle, we exposed the peptides ACTH1-10 and OVA257-264 to various superheating conditions, causing different degrees of decomposition. Optimized superheating conditions resulted in the entire peptide ladder sequence of the y-ions, allowing the amino acid sequence to be deduced from a single-stage mass spectrum. Thus, obtaining information in the same quality as from tandem mass spectrometry can be achieved by a single superheating step.

Dokumenty

BibTex


@article{BUT115137,
  author="Matthias O. {Altmayer} and Andreas {Manz} and Pavel {Neužil}",
  title="Microfluidic Superheating for Peptide Sequence Elucidation",
  annote="Herein, we introduce microfluidic superheating as a new method for peptide fragmentation prior to mass spectrometric analysis. The superheating conditions were found to be stable up to 240 C for more than 30 min without elevated pressure or boiling of the aqueous sample. As proof of principle, we exposed the peptides ACTH1-10 and OVA257-264 to various superheating conditions, causing different degrees of
decomposition. Optimized superheating conditions resulted in the entire peptide ladder sequence of the y-ions, allowing the amino acid sequence to be deduced from a single-stage mass spectrum. Thus, obtaining information in the same quality as from tandem mass spectrometry can be achieved by a single superheating step.",
  chapter="115137",
  doi="10.1021/acs.analchem.5b00189",
  howpublished="online",
  number="12",
  volume="87",
  year="2015",
  month="june",
  pages="5997--6003",
  type="journal article in Web of Science"
}