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Figure 1 | Molecular Neurodegeneration

Figure 1

From: Posttranslational modification and mutation of histidine 50 trigger alpha synuclein aggregation and toxicity

Figure 1

HNE modification of WT and H50 mutant aSyn. A) Recombinant WT aSyn treated with different concentrations of HNE (0 - 3000 μM) for 24 h was digested by GluC in order to measure HNE modification of the H50 containing peptide 47GVVHGVATVAE57 by MALDI-TOF analysis. The modification of this peptide (*observed monoisotopic mass to charge ratio m/z: 1038) by HNE leads to a mass increase of 156 Da (↓ observed monoisotopic m/z: 1194). B) aSyn H50Q and H50R mutations completely abolish HNE modification of the corresponding peptides containing the residue 50. Only unmodified peptides, i.e. 47GVVQGVATVAE57 (*observed monoisotopic m/z: 1029) of the H50Q aSyn and 47GVVRGVATVAE57 (*observed monoisotopic m/z: 1057) of the H50R aSyn, are observed. C) Recombinant full-length WT and H50Q/R aSyn were treated with different HNE concentrations for 24 h and analyzed by MALDI-TOF MS. Unmodified (*) and HNE-modified (↓) aSyn (WT, H50Q, and H50R) with a characteristic mass difference of 156 Da are indicated. H50Q/R mutations reduce the formation of aSyn-HNE-adducts, particularly they prevent the modification by HNE at low concentrations (50 - 200 μM).

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