Related Experiment Video
Updated: Jan 12, 2026

Quantification of Proteins Using Peptide Immunoaffinity Enrichment Coupled with Mass Spectrometry
Published on: July 31, 2011
Comments on "Untargeted LC-MS/MS profiling and semi-quantification of Gly-Pro-Yaa and Gly-Hyp-Yaa tripeptides in
Yuki Taga1, Masashi Kusubata1, Kazunori Mizuno1
1Nippi Research Institute of Biomatrix, 520-11 Kuwabara, Toride, Ibaraki, 302-0017, Japan.
Abstract:
A recent paper by Bai et al. (Talanta 295 (2025) 128317) presents an LC-MS method for the comprehensive profiling and semi-quantification of collagen-derived Gly-Pro-Yaa- and Gly-Hyp-Yaa-type tripeptides using precursor ion scanning, based on the specific detection of fragment ions at m/z 127 and 143, respectively. Although the concept of estimating the tripeptide content in commercial collagen hydrolysates is appealing, a careful reading of the manuscript raises several fundamental concerns regarding the methodology. In particular, the reported levels of Gly-Hyp-Yaa tripeptides appear unexpectedly high, possibly owing to misidentification with Gly-Leu/Ile-Yaa tripeptides, which generate an isobaric fragment ion at m/z 143. This possibility highlights the need for further validation and reexamination of this strategy.
More Related Videos
17:12Profiling of Methyltransferases and Other S-adenosyl-L-homocysteine-binding Proteins by Capture Compound Mass Spectrometry CCMS
Published on: December 20, 2010
07:28Enrichment of Extracellular Matrix Proteins from Tissues and Digestion into Peptides for Mass Spectrometry Analysis
Published on: July 23, 2015