Use of Engineered Unique Cysteine Residues to Facilitate Oriented Coupling of Proteins Directly to a Gold Substrate Academic Article uri icon

abstract

  • A prerequisite for any "lab on a chip" device that utilizes an electrical signal from the sensor protein is the ability to attach the protein in a specific orientation onto a conducting substrate. Here, we demonstrate the covalent attachment to a gold surface of light-harvesting membrane proteins, from Rhodobacter sphaeroides, via cysteine (Cys) residues engineered on either the cytoplasmic or periplasmic face. This simple directed attachment is superior in its ability to retain light-harvesting complex (LHC) function, when compared to a similar attachment procedure utilizing a self-assembled monolayer on gold. LH 1 has previously been observed to have superior photostability over LH 2 (Magis et al. [2010] Biochim. Biophys. Acta, 1798, 637-645); this characteristic is maintained even with the introduction of Cys residues.

authors

  • Magis, Gerhard J
  • Olsen, John D
  • Reynolds, Nicholas P
  • Leggett, Graham J
  • Hunter, C Neil
  • Aartsma, Thijs J
  • Frese, Raoul N

publication date

  • September 2011