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Determining Membrane Protein Topology Using Fluorescence Protease Protection FPP
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Carboxyl group-modified myoglobin shows membrane-permeabilizing activity.

Yi-Jun Shi1, Yuan-Chin Lee1, Liang-Jun Wang1

  • 1Institute of Biomedical Sciences, National Sun Yat-Sen University, Kaohsiung, 804, Taiwan.

Archives of Biochemistry and Biophysics
|August 3, 2022
PubMed
Summary

Modifying myoglobin (Mb) with semicarbazide creates SEM-Mb, a protein that can disrupt cell membranes. This structural change, caused by altering negative charges, unlocks membrane-permeabilizing activity.

Keywords:
Blocking of carboxyl groupMembrane-damaging activityMyoglobinStructural flexibility

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Membrane Biophysics

Background:

  • Myoglobin (Mb) is an oxygen-binding protein.
  • Understanding protein structure-function relationships is crucial.
  • Investigating protein modifications for novel activities is an active research area.

Purpose of the Study:

  • To determine if semicarbazide modification of myoglobin's carboxyl groups induces membrane-perturbing activity.
  • To elucidate the structural changes associated with this modification.
  • To understand the mechanism of membrane interaction.

Main Methods:

  • Mass spectrometry to confirm semicarbazide coupling.
  • Spectroscopic analyses (absorption, circular dichroism) to assess structural changes.
  • Fluorescence quenching and trifluoroethanol-induced transitions to evaluate protein flexibility.
  • Liposome and SDS micelle assays to study membrane interaction and permeability.

Main Results:

  • Semicarbazide modification (SEM-Mb) involved 19 of 22 carboxyl groups.
  • SEM-Mb lost its heme group and showed reduced α-helix content, increasing structural flexibility.
  • SEM-Mb, unlike native Mb, induced bilayer membrane permeability.
  • Both proteins bound lipids similarly, but SEM-Mb's Trp residues localized at the protein-lipid interface upon binding.

Conclusions:

  • Modification of negatively charged groups in Mb relieves structural constraints.
  • This modification switches Mb to a conformation with membrane-permeabilizing activity.
  • SEM-Mb offers a model for engineered proteins with altered membrane interaction properties.