Multi-laboratory analysis of the variability of shipped samples for proteomics following non-cooled international transport

Transporting biological samples such as cells or tissues is complicated by the need to maintain integrity and minimise modification and degradation, but this is economically costly as the samples must be shipped in a frozen state. This multi-laboratory study investigated sample variability introduce...

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Bibliographic Details
Published in:Analytical biochemistry 2018-05, Vol.548, p.60-65
Main Authors: Steffen, Pascal, Krisp, Christoph, Yi, Wang, Yang, Pengyuan, Molloy, Mark P., Schlüter, Hartmut
Format: Article
Language:English
Subjects:
Cell Line, Tumor
Chromatography, Liquid
Humans
LC-MS
Mass Spectrometry
Multi-laboratory
Neoplasm Proteins - chemistry
Neoplasm Proteins - metabolism
Neoplasms - chemistry
Neoplasms - metabolism
Peptides
Peptides - chemistry
Peptides - metabolism
Proteomics
Proteomics - methods
Specimen Handling - methods
Stability
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Summary:Transporting biological samples such as cells or tissues is complicated by the need to maintain integrity and minimise modification and degradation, but this is economically costly as the samples must be shipped in a frozen state. This multi-laboratory study investigated sample variability introduced by non-cooled transport of dried peptide samples for proteomic analysis using mass spectrometry. Human cancer cell tryptic lysates were proteolysed and dried in Australia and shipped by air to Europe and China. Samples were measured using label free mass spectrometry on similar LC-MS systems at all three sites. Preparation and analysis of the specimens in this manner resulted in only minor differences in protein identification and showed high quantitative reproducibility amongst the participating laboratories. We examined any impact on peptide chemical modification and report no discrepancies compared to the starting, non-shipped sample. We conclude that transport of non-cooled, dried peptides has negligible effect on sample integrity for downstream LC-MS analysis and therefore represents a cost-effective option to facilitate international proteomic collaborations. Data is available via ProteomeXchange with identifier PXD008160. •First proteomic study to examine the impact of transport of non-cooled, dried peptides derived from biological samples.•Dried peptides are highly stable when transported without cooling for LC-MS/MS analysis.•Shipping of dried tryptic peptides has any significant impact on peptide chemical modification.
ISSN:0003-2697
1096-0309
DOI:10.1016/j.ab.2018.02.026