Related Experiment Video
Updated: May 17, 2026
A Plasma Sample Preparation for Mass Spectrometry using an Automated Workstation
Published on: April 24, 2020
An automated plasma protein fractionation design: high-throughput perspectives for proteomic analysis
Claudia Boccardi1, Silvia Rocchiccioli, Antonella Cecchettini
1Institute of Clinical Physiology-CNR, Via Moruzzi 1, 56124 Pisa, Italy.
Background:
Human plasma, representing the most complete record of the individual phenotype, is an appealing sample for proteomics analysis in clinical applications. Up to today, the major obstacle in a proteomics study of plasma is the large dynamic range of protein concentration and the efforts of many researchers focused on the resolution of this important drawback.
Findings:
In this study, proteins from pooled plasma samples were fractionated according to their chemical characteristics on a home-designed SPE automated platform. The resulting fractions were digested and further resolved by reversed-phase liquid chromatography coupled with MALDI TOF/TOF mass spectrometry. A total of 712 proteins were successfully identified until a concentration level of ng/mL. Pearson correlation coefficient was used to test reproducibility.
Conclusions:
Our multidimensional fractionation approach reduced the analysis time (2 days are enough to process 16 plasma samples filling a 96-well plate) over the conventional gel-electrophoresis or multi-LC column based methods. The robotic processing, avoiding contaminants or lack of sample handling skill, promises highly reproducible specimen analyses (more than 85% Pearson correlation). The automated platform here presented is flexible and easily modulated changing fractioning elements or detectors.
