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Journal of APPLIED BIOMEDICINE
ISSN 1214-0287 (on-line)
ISSN 1214-021X (printed)

Volume 2 (2004), No 2, p 113-117




MALDI-TOF mass spectrometric properties of humanin-like peptides

Klara Novotna, Ondrej Sedo, Josef Havel

Address: Josef Havel, Department of Analytical Chemistry, Faculty of Science, Masaryk University, Kotlarska 2, 611 37 Brno, Czech Republic
havel@chemi.muni.cz

Received 21st January 2004.
Revised 19th February 2004.
Published online 16th April 2004.

Full text article (pdf)

SUMMARY
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 humaninlike peptides.

KEY WORDS
[G14]-humanin; humanin derivatives; MALDI-TOF MS; PSD; peptide oxidation


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CITED

Novotna K, Havlis J, Havel J: HPLC separation-of neuroprotective peptides - General approach, towards optimization: experimental sesign combined with artificial neural networks. Pept 2004, Proceedings - Bridges Between Disciplines 469-470, 2005.

Novotna K, Havlis J, Havel J: Optimisation of high performance liquid chromatography separation of neuroprotective peptides - Fractional experimental designs combined with artificial neural networks. J Chromatogr A 1096:50-57, 2005.


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