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Nonionic, Cleavable Surfactant for Top-Down Proteomics.

Kyle A Brown1,2, Morgan K Gugger1, Zhen Yu1

  • 1Department of Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, United States.

Analytical Chemistry
|January 6, 2023
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Summary
This summary is machine-generated.

A new cleavable surfactant, n-decyl-disulfide-β-D-maltoside (DSSM), enables non-denaturing protein extraction for mass spectrometry. DSSM facilitates top-down proteomics by allowing easy surfactant removal, improving analysis of proteins and complexes.

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Area of Science:

  • Biochemistry
  • Analytical Chemistry
  • Proteomics

Background:

  • Nonionic surfactants like n-dodecyl-β-D-maltoside (DDM) are crucial for protein extraction and stabilization in structural biology.
  • However, surfactants can interfere with sensitive electrospray ionization (ESI)-mass spectrometry (MS) analyses.
  • This interference poses challenges for top-down proteomics and structural studies.

Purpose of the Study:

  • To introduce a novel nonionic, cleavable surfactant, n-decyl-disulfide-β-D-maltoside (DSSM).
  • To demonstrate DSSM's utility in top-down proteomics and structural biology.
  • To provide a surfactant compatible with ESI-MS and RPLC-MS analysis.

Main Methods:

  • Synthesis and characterization of DSSM, a disulfide-containing analog of DDM.
  • Compatibility testing of DSSM with direct ESI-MS and reversed-phase liquid chromatography (RPLC)-MS.
  • Application of DSSM for top-down proteomic analysis of membrane proteins and endogenous proteins.

Main Results:

  • DSSM effectively mimics DDM's properties for protein solubilization and stabilization.
  • The disulfide bond in DSSM allows for facile cleavage and removal prior to or during MS analysis.
  • DSSM demonstrated compatibility with ESI-MS and RPLC-MS, enabling analysis of proteins and complexes.
  • Successful top-down proteomic characterization of membrane proteins (ion channel, GPCR) and endogenous proteins was achieved.
  • Determination of sequence variations and posttranslational modifications (PTMs) was facilitated by DSSM.

Conclusions:

  • DSSM is a valuable nonionic, cleavable surfactant for top-down proteomics.
  • It offers a compatible alternative to DDM in mass spectrometry-based protein studies.
  • DSSM facilitates the analysis of challenging protein samples, including membrane proteins and endogenous lysates.