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

Pascal Steffen, Christoph Krisp, Wang Yi, Pengyuan Yang, Mark P. Molloy, Hartmut Schlüter

Research output: Contribution to journalArticleResearchpeer-review

Abstract

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.

LanguageEnglish
Pages60-65
Number of pages6
JournalAnalytical Biochemistry
Volume548
DOIs
Publication statusPublished - 1 May 2018

Fingerprint

Proteomics
Peptides
Mass spectrometry
Mass Spectrometry
Chemical modification
Labels
China
Air
Cells
Tissue
Costs and Cost Analysis
Degradation
Costs
Neoplasms
Proteins

Cite this

@article{427f18cf9da3487eb4271d39ab643e6a,
title = "Multi-laboratory analysis of the variability of shipped samples for proteomics following non-cooled international transport",
abstract = "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.",
keywords = "Proteomics, Peptides, Stability, LC-MS, Multi-laboratory",
author = "Pascal Steffen and Christoph Krisp and Wang Yi and Pengyuan Yang and Molloy, {Mark P.} and Hartmut Schl{\"u}ter",
year = "2018",
month = "5",
day = "1",
doi = "10.1016/j.ab.2018.02.026",
language = "English",
volume = "548",
pages = "60--65",
journal = "Analytical Biochemistry",
issn = "0003-2697",
publisher = "Academic Press",

}

Multi-laboratory analysis of the variability of shipped samples for proteomics following non-cooled international transport. / Steffen, Pascal; Krisp, Christoph; Yi, Wang; Yang, Pengyuan; Molloy, Mark P.; Schlüter, Hartmut.

In: Analytical Biochemistry, Vol. 548, 01.05.2018, p. 60-65.

Research output: Contribution to journalArticleResearchpeer-review

TY - JOUR

T1 - Multi-laboratory analysis of the variability of shipped samples for proteomics following non-cooled international transport

AU - Steffen,Pascal

AU - Krisp,Christoph

AU - Yi,Wang

AU - Yang,Pengyuan

AU - Molloy,Mark P.

AU - Schlüter,Hartmut

PY - 2018/5/1

Y1 - 2018/5/1

N2 - 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.

AB - 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.

KW - Proteomics

KW - Peptides

KW - Stability

KW - LC-MS

KW - Multi-laboratory

UR - http://www.scopus.com/inward/record.url?scp=85042659119&partnerID=8YFLogxK

U2 - 10.1016/j.ab.2018.02.026

DO - 10.1016/j.ab.2018.02.026

M3 - Article

VL - 548

SP - 60

EP - 65

JO - Analytical Biochemistry

T2 - Analytical Biochemistry

JF - Analytical Biochemistry

SN - 0003-2697

ER -