Rapid tryptic peptide mapping of human serum albumin using DI-MS/MS ALL .
Ke ZhangXingcheng GongQian WangPengfei TuJun LiYuelin SongPublished in: RSC advances (2022)
In recent decades, proteinic drugs, in particular monoclonal antibodies, are taking the leading role of small molecule drugs, and peptide mapping relying on liquid chromatography-tandem mass spectrometry (LC-MS/MS) is an emerging approach to substitute the role of a ligand-binding assay for the quality control of the proteinic drugs. However, such LC-MS/MS approaches extensively suffer from time-intensive measurements, leading to a limited throughput. To achieve accelerated measurements, here, the potential of DI-MS/MS ALL towards tryptic peptide mapping was evaluated through comparing with well-defined LC-MS/MS means, and human serum albumin (HSA) was employed as the representative protein for applicability illustration. Among the 55 tryptic peptides theoretically suggested by Skyline software, 47 were successfully captured by DI-MS/MS ALL through acquiring the desired MS 2 spectra, in comparison to 51 detected by LC-MS/MS. DI-MS/MS ALL measurements merely took 5 min, which was dramatically superior to the LC-MS/MS assay. Noteworthily, different from fruitful multi-charged MS 1 signals for LC-MS/MS, most quasi-molecular ions received lower charged states. DI-MS/MS ALL also possessed advantages such as lower solvent consumption and facile instrumentation; however, more sample was consumed. In conclusion, DI-MS/MS ALL is eligible to act as an alternative analytical tool for LC-MS/MS towards the peptide mapping of proteinic drugs, particularly when a heavy measurement workload.
Keyphrases
- ms ms
- liquid chromatography tandem mass spectrometry
- human serum albumin
- biofilm formation
- high resolution
- small molecule
- quality control
- high throughput
- multiple sclerosis
- mass spectrometry
- staphylococcus aureus
- risk assessment
- high performance liquid chromatography
- cystic fibrosis
- single molecule
- human health
- single cell
- loop mediated isothermal amplification