Inherently Tunable Electrostatic Assembly of Membrane Proteins

• Published in: Nano letters Vol. 8; no. 1; pp. 333 - 339
• Main Authors: Liang, Hongjun, Whited, Gregg, Nguyen, Chi, Okerlund, Adam, Stucky, Galen D
• Format: Journal Article
• Language: English
• Published: Washington, DC American Chemical Society 01-01-2008
• Subjects: Biological and medical sciences; Biotechnology; Cross-disciplinary physics: materials science; rheology; Exact sciences and technology; Fundamental and applied biological sciences. Psychology; Materials science; Membrane Proteins - chemistry; Methods of nanofabrication; Methods. Procedures. Technologies; Others; Physics; Static Electricity; Various methods and equipments; Nanometer scale; Electrostatic effect; Crystallization; Electrostatic interaction; Amino acids; Lipids; Carbon monoxide; Arrays; Nanomaterial synthesis; Membrane proteins
• ISSN: 1530-6984; 1530-6992
• DOI: 10.1021/nl0729173

Membrane proteins are a class of nanoscopic entities that control the matter, energy, and information transport across cellular boundaries. Electrostatic interactions are shown to direct the rapid co-assembly of proteorhodopsin (PR) and lipids into long-range crystalline arrays. The roles of inherent charge variations on lipid membranes and PR variants with different compositions are examined by tuning recombinant PR variants with different extramembrane domain sizes and charged amino acid substitutions, lipid membrane compositions, and lipid-to-PR stoichiometric ratios. Rational control of this predominantly electrostatic assembly for PR crystallization is demonstrated, and the same principles should be applicable to the assembly and crystallization of other integral membrane proteins.