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Synthetic fluoro peptides in neat solvent and complex proteome background

ABSTRACT: This dataset was generated to model discovery of uncommon and non-canonical PTM by agnostic analysis. Synthetic DFSAFILVEFCR peptides were obtained in three chemoforms, all with carbamidomethylated C12: 1) with unmodified phenylalanines, 2) with fluoro-F2, and 3) with fluoro-F11. Peptide composition and chemical modifications were confirmed using mass spectrometry. Peptides were analyzed in neat solvent for sequence and modification confirmation, and in the context of AML cell tryptic proteome.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Suspension Culture

DISEASE(S): Acute Leukemia

SUBMITTER: Alex Kentsis

LAB HEAD: Alex Kentsis

PROVIDER: PXD019827 | Pride | 2021-07-22

REPOSITORIES: Pride

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Discovery of Protein Modifications Using Differential Tandem Mass Spectrometry Proteomics.

Cifani Paolo P Li Zhi Z Luo Danmeng D Grivainis Mark M Intlekofer Andrew M AM Fenyö David D Kentsis Alex A

Journal of proteome research 20210322 4

Recent studies have revealed diverse amino acid, post-translational, and noncanonical modifications of proteins in diverse organisms and tissues. However, their unbiased detection and analysis remain hindered by technical limitations. Here, we present a spectral alignment method for the identification of protein modifications using high-resolution mass spectrometry proteomics. Termed SAMPEI for spectral alignment-based modified peptide identification, this open-source algorithm is designed for t ...[more]

PMID: 33749263

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