J Appl Biomed 2:111-115, 2004 | DOI: 10.32725/jab.2004.013

MALDI-TOF mass spectrometric properties of humanin-like peptides

Klára Novotná, Ondrej Šedo, Josef Havel*
Department of Analytical Chemistry, Faculty of Science, Masaryk University, Brno, Czech Republic

The possibilities of MALDI-TOF mass spectrometric analysis of new neuro-protective peptide [G14]-humanin (HNG) and similar compounds are studied with the aim of finding optimal conditions for the determination of these peptides. Acidification and washing of HNG samples using 5% (v/v) formic acid is necessary to reach a detection limit similar to other peptides. The sensitivity of HNG determination is decreased in the oxidative environment as the peptide yields oxidation of methionine and cysteine forming several species, including a disulfide dimer. During Post-source Decay (PSD) it was found that intense cleavage between Asp and Leu in HNG reduces the possibility of detecting other fragments. Better sequence coverage is gained from shorter humanin-like peptides.

Keywords: [G14]-humanin; humanin derivatives; MALDI-TOF MS; PSD; peptide oxidation

Received: January 21, 2004; Revised: February 19, 2004; Published: July 31, 2004  Show citation

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Novotná K, Šedo O, Havel J. MALDI-TOF mass spectrometric properties of humanin-like peptides. J Appl Biomed. 2004;2(2):111-115. doi: 10.32725/jab.2004.013.
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