Picodiscs for facile protein-glycolipid interaction analysis

Aneika C. Leney; Reza Rezaei Darestani; Jun Li; Sanaz Nikjah; Elena N. Kitova; Chunxia Zou; Christopher W. Cairo; Zi Jian Xiong; Gilbert G. Privé; John S. Klassen

doi:10.1021/acs.analchem.5b00170

Picodiscs for facile protein-glycolipid interaction analysis

Aneika C. Leney, Reza Rezaei Darestani, Jun Li, Sanaz Nikjah, Elena N. Kitova, Chunxia Zou, Christopher W. Cairo, Zi Jian Xiong, Gilbert G. Privé, John S. Klassen^*

^*Corresponding author for this work

Biosciences

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

21 Citations (Scopus)

Abstract

Protein interactions with glycolipids are implicated in diverse cellular processes. However, the study of protein-glycolipid complexes remains a significant experimental challenge. Here, we describe a powerful new assay that combines electrospray ionization mass spectrometry (ESI-MS) and picodiscs, which are composed of human sphingolipid activator protein saposin A and a small number of phospholipids, to display glycolipids in a lipid environment for protein-glycolipid interaction studies in aqueous solution. Time-resolved measurements of enzyme catalyzed hydrolysis of glycolipid substrates and the detection of low, moderate, and high affinity protein-glycolipid interactions serve to demonstrate the reliability and versatility of the assay.

Original language	English
Pages (from-to)	4402-4408
Number of pages	7
Journal	Analytical Chemistry
Volume	87
Issue number	8
Early online date	9 Apr 2015
DOIs	https://doi.org/10.1021/acs.analchem.5b00170
Publication status	Published - 21 Apr 2015

ASJC Scopus subject areas

Analytical Chemistry

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Cite this

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title = "Picodiscs for facile protein-glycolipid interaction analysis",

abstract = "Protein interactions with glycolipids are implicated in diverse cellular processes. However, the study of protein-glycolipid complexes remains a significant experimental challenge. Here, we describe a powerful new assay that combines electrospray ionization mass spectrometry (ESI-MS) and picodiscs, which are composed of human sphingolipid activator protein saposin A and a small number of phospholipids, to display glycolipids in a lipid environment for protein-glycolipid interaction studies in aqueous solution. Time-resolved measurements of enzyme catalyzed hydrolysis of glycolipid substrates and the detection of low, moderate, and high affinity protein-glycolipid interactions serve to demonstrate the reliability and versatility of the assay.",

author = "Leney, {Aneika C.} and {Rezaei Darestani}, Reza and Jun Li and Sanaz Nikjah and Kitova, {Elena N.} and Chunxia Zou and Cairo, {Christopher W.} and Xiong, {Zi Jian} and Priv{\'e}, {Gilbert G.} and Klassen, {John S.}",

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doi = "10.1021/acs.analchem.5b00170",

language = "English",

volume = "87",

pages = "4402--4408",

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T1 - Picodiscs for facile protein-glycolipid interaction analysis

AU - Leney, Aneika C.

AU - Rezaei Darestani, Reza

AU - Li, Jun

AU - Nikjah, Sanaz

AU - Kitova, Elena N.

AU - Zou, Chunxia

AU - Cairo, Christopher W.

AU - Xiong, Zi Jian

AU - Privé, Gilbert G.

AU - Klassen, John S.

PY - 2015/4/21

Y1 - 2015/4/21

N2 - Protein interactions with glycolipids are implicated in diverse cellular processes. However, the study of protein-glycolipid complexes remains a significant experimental challenge. Here, we describe a powerful new assay that combines electrospray ionization mass spectrometry (ESI-MS) and picodiscs, which are composed of human sphingolipid activator protein saposin A and a small number of phospholipids, to display glycolipids in a lipid environment for protein-glycolipid interaction studies in aqueous solution. Time-resolved measurements of enzyme catalyzed hydrolysis of glycolipid substrates and the detection of low, moderate, and high affinity protein-glycolipid interactions serve to demonstrate the reliability and versatility of the assay.

AB - Protein interactions with glycolipids are implicated in diverse cellular processes. However, the study of protein-glycolipid complexes remains a significant experimental challenge. Here, we describe a powerful new assay that combines electrospray ionization mass spectrometry (ESI-MS) and picodiscs, which are composed of human sphingolipid activator protein saposin A and a small number of phospholipids, to display glycolipids in a lipid environment for protein-glycolipid interaction studies in aqueous solution. Time-resolved measurements of enzyme catalyzed hydrolysis of glycolipid substrates and the detection of low, moderate, and high affinity protein-glycolipid interactions serve to demonstrate the reliability and versatility of the assay.

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DO - 10.1021/acs.analchem.5b00170

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JO - Analytical Chemistry

JF - Analytical Chemistry

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Picodiscs for facile protein-glycolipid interaction analysis

Abstract

ASJC Scopus subject areas

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