Ultrathin films of oriented bacteriorhodopsin: Nanostructured films for investigating the primary photoevent in vision processes

Rigoberto C. Advincula*, Mi Kyoung Park

*Corresponding author for this work

Research output: Chapter in Book/Report/Conference proceedingConference contribution


In this work, a protocol for investigating Bacteriorhodopsin (BR) biomimetic systems as ultrathin films is presented. BR is one of the most well studied proteins important for investigating the primary photo-event in vision processes. The use of macromolecular assembly approaches for deposition onto solid support substrates, e.g. SiOx, gold- or ITO-coated glass (electrode) provide advantages in that surface sensitive measurements can be used to correlate photocurrent generation, photoelectric response, pH change, chromophore behavior, etc. with protein orientation at interfaces. Membrane and protein morphology were correlated to measurements using surface sensitive techniques, such as atomic force microscopy (AFM), ellipsometry, quartz crystal microbalance (QCM), etc. on solid-substrate systems. These studies can lead to applications in optobioelectronic devices (biosensors) including patterning in transducer array configurations, where the film structure is important. Hybrid films are possible with supramolecular assembly approaches, e.g. adsorption of membrane with lipidbilayers. We report our initial results on highly ordered and oriented BR protein arrays of controlled thickness, layer order, and orientation. This was done primarily using the alternate polyelectrolyte deposition (APD) or layer-by-layer (LbL) approach to functionalize substrate surfaces.

Original languageEnglish
Title of host publicationMolecular and Biomolecular Electronics
Number of pages6
Publication statusPublished - 2001
Externally publishedYes
Event2001 MRS Spring Meeting - San Francisco, CA
Duration: 2001 Apr 162001 Apr 20


Other2001 MRS Spring Meeting
CitySan Francisco, CA

ASJC Scopus subject areas

  • Electronic, Optical and Magnetic Materials


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