Lack of association between a cationic protein and a cationic fluorosurfactant

Langmuir. 2007 Jan 16;23(2):771-5. doi: 10.1021/la062469z.

Abstract

Surface tension, 19F and 1H NMR spectroscopy, and cryotransmission electron microscopy are used to characterize the state of association in aqueous solutions of a fluorosurfactant CF3(CF2)nSO2NH(CH2)3-4N(CH3)3+ I- (n = 8, 6) with and without lysozyme added. In the absence of lysozyme, we find monomers, small aggregates, and large vesicles to coexist, with the individual fluorosurfactant molecules exchanging slowly (>1 ms) among those states. When both lysozyme and fluorosurfactant are present in the solution, they have no measurable influence on the physical state of the other. In contrast, a hydrogenated cationic surfactant with the same headgroup, hexadecyltrimethylammonium bromide, is shown to associate to lysozyme.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cations
  • Cetrimonium
  • Cetrimonium Compounds / chemistry
  • Chemistry, Physical / methods
  • Cryoelectron Microscopy
  • Hydrogen Bonding
  • Magnetic Resonance Spectroscopy
  • Microscopy, Electron, Transmission
  • Molecular Structure
  • Muramidase / chemistry*
  • Protein Folding
  • Surface Properties
  • Surface Tension
  • Surface-Active Agents / chemistry*

Substances

  • Cations
  • Cetrimonium Compounds
  • Surface-Active Agents
  • Muramidase
  • Cetrimonium