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Peptide artificial formylation in bottom–up proteomics analyses

ABSTRACT: The primary objective of this study was to explain excessive formylation rate of peptides that did not come in contact with concentrated formic acid.

INSTRUMENT(S): Q Exactive HF-X

ORGANISM(S): Francisella Tularensis Subsp. Holarctica

SUBMITTER: Juraj Lenco

LAB HEAD: Juraj Lenco, Ph.D.

PROVIDER: PXD016597 | Pride | 2020-06-10

REPOSITORIES: Pride

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			Action	DRS
	DataDescription.xlsx	Xlsx
	JL705_JL697_FtularensisLVS_Digest_2uGin1uL_0l5uL_000min_01.msf	Msf
	JL705_JL697_FtularensisLVS_Digest_2uGin1uL_0l5uL_000min_01.raw	Raw
	JL705_JL697_FtularensisLVS_Digest_2uGin1uL_0l5uL_000min_02.msf	Msf
	JL705_JL697_FtularensisLVS_Digest_2uGin1uL_0l5uL_000min_02.raw	Raw

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Publications

Dissolving Peptides in 0.1% Formic Acid Brings Risk of Artificial Formylation.

Lenčo Juraj J Khalikova Maria A MA Švec František F

Journal of proteome research 20200220 3

The ability of concentrated formic acid to formylate reactive amino acid residues is known from previous reports. In contrast, solvents containing a low concentration of formic acid are generally recognized as a safe environment for proteomic applications. The primary objective of this study was to explain the excessive formylation rate in tryptic peptides that did not come into contact with concentrated formic acid. We found out that the peptide formylation was associated with dissolving the pe ...[more]

PMID: 32068400

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