Langmuir monolayer characterization of metal chelating lipids for protein targeting to membranes

Daniel W. Pack, Frances H. Arnold

Research output: Contribution to journalArticlepeer-review

32 Scopus citations


Targeting and organization of proteins on lipid membranes led to applications in both biological and materials sciences. Coordination of membrane-bound metal ions by surface histidine residues provides a general method for targeting of proteins to membrane surfaces. Here we report the Langmuir monolayer properties of a new class of metal-chelating lipids. The lipids utilize the metal chelator iminodiacetate (IDA) as the hydrophilic headgroup, allowing display of divalent transition metal ions on the aqueous side of the membrane. Changes in surface pressure-molecular area isotherms were used to observe metal binding, and an association constant for Cu2+ binding to the IDA lipids of 107-8 M-1 was estimated. The ability to control binding site density is important for many applications. The IDA lipid was found to be miscible with both distearoylphosphocholine (DSPC) and 1-stearoyl-2-oleoyl-phosphocholine (SOPC) at most compositions and surface pressures.

Original languageEnglish
Pages (from-to)135-152
Number of pages18
JournalChemistry and Physics of Lipids
Issue number2
StatePublished - Apr 25 1997

Bibliographical note

Funding Information:
The DPIDA lipid was kindly synthesized by Dr. Chao-Tsen Chen. This work was supported by the Office of Naval Research (N00014-92-J-1178). D.W.P. was a Landau fellow and is supported by a training fellowship from the National Institute of General Medical Sciences, NRSA Award 1 T32 GM 08346-01.


  • Fluorescence microscopy
  • Functionalized surfaces
  • Iminodiacetate-copper
  • Molecular recognition
  • Protein immobilization

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Organic Chemistry
  • Cell Biology


Dive into the research topics of 'Langmuir monolayer characterization of metal chelating lipids for protein targeting to membranes'. Together they form a unique fingerprint.

Cite this