Surfactant-free purification of membrane protein complexes from bacteria: application to the staphylococcal penicillin-binding protein complex PBP2/PBP2a

Nanotechnology. 2014 Jul 18;25(28):285101. doi: 10.1088/0957-4484/25/28/285101. Epub 2014 Jun 27.


Surfactant-mediated removal of proteins from biomembranes invariably results in partial or complete loss of function and disassembly of multi-protein complexes. We determined the capacity of styrene-co-maleic acid (SMA) co-polymer to remove components of the cell division machinery from the membrane of drug-resistant staphylococcal cells. SMA-lipid nanoparticles solubilized FtsZ-PBP2-PBP2a complexes from intact cells, demonstrating the close physical proximity of these proteins within the lipid bilayer. Exposure of bacteria to (-)-epicatechin gallate, a polyphenolic agent that abolishes β-lactam resistance in staphylococci, disrupted the association between PBP2 and PBP2a. Thus, SMA purification provides a means to remove native integral membrane protein assemblages with minimal physical disruption and shows promise as a tool for the interrogation of molecular aspects of bacterial membrane protein structure and function.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Catechin / analogs & derivatives
  • Catechin / chemistry
  • Cell Division / physiology
  • Lipid Bilayers / chemistry
  • Maleates / chemistry
  • Membrane Proteins / chemistry*
  • Penicillin-Binding Proteins / chemistry*
  • Peptide Synthases / chemistry*
  • Polystyrenes / chemistry
  • Staphylococcus aureus / chemistry*
  • Surface-Active Agents / chemistry*


  • Bacterial Proteins
  • Lipid Bilayers
  • Maleates
  • Membrane Proteins
  • Penicillin-Binding Proteins
  • Polystyrenes
  • Surface-Active Agents
  • penicillin-binding protein 2a, Streptococcus
  • styrene-maleic acid polymer
  • Catechin
  • epicatechin gallate
  • Peptide Synthases