Native liquid extraction surface analysis mass spectrometry: analysis of noncovalent protein complexes directly from dried substrates

Nicholas J. Martin; Rian L. Griffiths; Rebecca L. Edwards; Helen J. Cooper

doi:10.1007/s13361-015-1152-8

Native liquid extraction surface analysis mass spectrometry: analysis of noncovalent protein complexes directly from dried substrates

Nicholas J. Martin, Rian L. Griffiths, Rebecca L. Edwards, Helen J. Cooper

Biosciences

Research output: Contribution to journal › Article › peer-review

30 Citations (Scopus)

218 Downloads (Pure)

Abstract

Liquid extraction surface analysis (LESA) mass spectrometry is a promising tool for the analysis of intact proteins from biological substrates. Here, we demonstrate native LESA mass spectrometry of noncovalent protein complexes of myoglobin and hemoglobin from a range of surfaces. Holomyoglobin, in which apomyoglobin is noncovalently bound to the prosthetic heme group, was observed following LESA mass spectrometry of myoglobin dried onto glass and polyvinylidene fluoride surfaces. Tetrameric hemoglobin [(αβ)₂^4H] was observed following LESA mass spectrometry of hemoglobin dried onto glass and polyvinylidene fluoride (PVDF) surfaces, and from dried blood spots (DBS) on filter paper. Heme-bound dimers and monomers were also observed. The 'contact' LESA approach was particularly suitable for the analysis of hemoglobin tetramers from DBS.

Original language	English
Pages (from-to)	1320-1327
Number of pages	8
Journal	Journal of the American Society for Mass Spectrometry
Volume	26
Issue number	8
Early online date	20 May 2015
DOIs	https://doi.org/10.1007/s13361-015-1152-8
Publication status	Published - 1 Aug 2015

Keywords

Native mass spectrometry
Proteins
Liquid extraction surface analysis
LESA
Liquid microjunction sampling
Direct surface sampling
Dried blood spots

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10.1007/s13361-015-1152-8Licence: Creative Commons: Attribution (CC BY)

Martin_et_al_Native_liquid_extraction_surface_analysis_ASMS_2015
Eligibility for repository : checked 20/07/2015
Final published version, 1.31 MBLicence: Creative Commons: Attribution (CC BY)

NISA: Novel approaches for in situ analysis of biomolecules
Cooper, H. (Principal Investigator)
Engineering & Physical Science Research Council
1/06/14 → 31/05/19
Project: Research
Chemistry at Birmingham: a Response to the EPSRC Call: Core Capability for Chemistry Research
Simpkins, N. (Principal Investigator), Anderson, P. (Co-Investigator), Britton, M. (Co-Investigator), Bunch, J. (Co-Investigator), Preece, J. (Co-Investigator) & Slater, P. (Co-Investigator)
Engineering & Physical Science Research Council
1/01/13 → 31/03/13
Project: Research

Cite this

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title = "Native liquid extraction surface analysis mass spectrometry: analysis of noncovalent protein complexes directly from dried substrates",

abstract = "Liquid extraction surface analysis (LESA) mass spectrometry is a promising tool for the analysis of intact proteins from biological substrates. Here, we demonstrate native LESA mass spectrometry of noncovalent protein complexes of myoglobin and hemoglobin from a range of surfaces. Holomyoglobin, in which apomyoglobin is noncovalently bound to the prosthetic heme group, was observed following LESA mass spectrometry of myoglobin dried onto glass and polyvinylidene fluoride surfaces. Tetrameric hemoglobin [(αβ)24H] was observed following LESA mass spectrometry of hemoglobin dried onto glass and polyvinylidene fluoride (PVDF) surfaces, and from dried blood spots (DBS) on filter paper. Heme-bound dimers and monomers were also observed. The 'contact' LESA approach was particularly suitable for the analysis of hemoglobin tetramers from DBS. ",

keywords = "Native mass spectrometry, Proteins, Liquid extraction surface analysis, LESA, Liquid microjunction sampling, Direct surface sampling, Dried blood spots",

author = "Martin, {Nicholas J.} and Griffiths, {Rian L.} and Edwards, {Rebecca L.} and Cooper, {Helen J.}",

year = "2015",

month = aug,

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doi = "10.1007/s13361-015-1152-8",

language = "English",

volume = "26",

pages = "1320--1327",

journal = "Journal of the American Society for Mass Spectrometry",

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Native liquid extraction surface analysis mass spectrometry: analysis of noncovalent protein complexes directly from dried substrates. / Martin, Nicholas J.; Griffiths, Rian L.; Edwards, Rebecca L. et al.
In: Journal of the American Society for Mass Spectrometry, Vol. 26, No. 8, 01.08.2015, p. 1320-1327.

Research output: Contribution to journal › Article › peer-review

TY - JOUR

T1 - Native liquid extraction surface analysis mass spectrometry

T2 - analysis of noncovalent protein complexes directly from dried substrates

AU - Martin, Nicholas J.

AU - Griffiths, Rian L.

AU - Edwards, Rebecca L.

AU - Cooper, Helen J.

PY - 2015/8/1

Y1 - 2015/8/1

N2 - Liquid extraction surface analysis (LESA) mass spectrometry is a promising tool for the analysis of intact proteins from biological substrates. Here, we demonstrate native LESA mass spectrometry of noncovalent protein complexes of myoglobin and hemoglobin from a range of surfaces. Holomyoglobin, in which apomyoglobin is noncovalently bound to the prosthetic heme group, was observed following LESA mass spectrometry of myoglobin dried onto glass and polyvinylidene fluoride surfaces. Tetrameric hemoglobin [(αβ)24H] was observed following LESA mass spectrometry of hemoglobin dried onto glass and polyvinylidene fluoride (PVDF) surfaces, and from dried blood spots (DBS) on filter paper. Heme-bound dimers and monomers were also observed. The 'contact' LESA approach was particularly suitable for the analysis of hemoglobin tetramers from DBS.

AB - Liquid extraction surface analysis (LESA) mass spectrometry is a promising tool for the analysis of intact proteins from biological substrates. Here, we demonstrate native LESA mass spectrometry of noncovalent protein complexes of myoglobin and hemoglobin from a range of surfaces. Holomyoglobin, in which apomyoglobin is noncovalently bound to the prosthetic heme group, was observed following LESA mass spectrometry of myoglobin dried onto glass and polyvinylidene fluoride surfaces. Tetrameric hemoglobin [(αβ)24H] was observed following LESA mass spectrometry of hemoglobin dried onto glass and polyvinylidene fluoride (PVDF) surfaces, and from dried blood spots (DBS) on filter paper. Heme-bound dimers and monomers were also observed. The 'contact' LESA approach was particularly suitable for the analysis of hemoglobin tetramers from DBS.

KW - Native mass spectrometry

KW - Proteins

KW - Liquid extraction surface analysis

KW - LESA

KW - Liquid microjunction sampling

KW - Direct surface sampling

KW - Dried blood spots

U2 - 10.1007/s13361-015-1152-8

DO - 10.1007/s13361-015-1152-8

M3 - Article

C2 - 25990922

SN - 1044-0305

VL - 26

SP - 1320

EP - 1327

JO - Journal of the American Society for Mass Spectrometry

JF - Journal of the American Society for Mass Spectrometry

IS - 8

ER -

Native liquid extraction surface analysis mass spectrometry: analysis of noncovalent protein complexes directly from dried substrates

Abstract

Keywords

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Projects

NISA: Novel approaches for in situ analysis of biomolecules

Chemistry at Birmingham: a Response to the EPSRC Call: Core Capability for Chemistry Research

Cite this