ArticleJournal of biomolecular techniques : JBT2013
The use of ammonium formate as a mobile-phase modifier for LC-MS/MS analysis of tryptic digests.
Article in Journal of biomolecular techniques : JBT, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed, 42 citations in OpenAlex.
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- Simultaneous Analysis of Fenthion and Its Five Metabolites in Produce Using Ultra-High Performance Liquid Chromatography-Tandem Mass Spectrometry.Molecules (Basel, Switzerland) · 2020Article
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- A rapid and sensitive liquid chromatography-tandem mass spectrometric method for the determination of hederasaponin B in rat plasma: Application to a pharmacokinetic study.Asian journal of pharmaceutical sciences · 2017Article
- Optimized superficially porous particles for protein separations.Journal of chromatography. A · 2013Article
- Article
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3 authors at 1 institution in 1 country.
Funding
Abstract
A major challenge facing current mass spectrometry (MS)-based proteomics research is the large concentration range displayed in biological systems, which far exceeds the dynamic range of commonly available mass spectrometers. One approach to overcome this limitation is to improve online reversed-phase liquid chromatography (RP-LC) separation methodologies. LC mobile-phase modifiers are used to improve peak shape and increase sample load tolerance. Trifluoroacetic acid (TFA) is a commonly used mobile-phase modifier, as it produces peptide separations that are far superior to other additives. However, TFA leads to signal suppression when incorporated with electrospray ionization (ESI), and thus, other modifiers, such as formic acid (FA), are used for LC-MS applications. FA exhibits significantly less signal suppression, but is not as effective of a modifier as TFA. An alternative mobile-phase modifier is the combination of FA and ammonium formate (AF), which has been shown to improve peptide separations. The ESI-MS compatibility of this modifier has not been investigated, particularly for proteomic applications. This work compares the separation metrics of mobile phases modified with FA and FA/AF and explores the use of FA/AF for the LC-MS analysis of tryptic digests. Standard tryptic-digest peptides were used for comparative analysis of peak capacity and sample load tolerance. The compatibility of FA/AF in proteomic applications was examined with the analysis of soluble proteins from canine prostate carcinoma tissue. Overall, the use of FA/AF improved online RP-LC separations and led to significant increases in peptide identifications with improved protein sequence coverage.
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