Paper
19 April 2002 Bacteriorhodopsin-based photochromic pigments for optical security applications
Norbert A. Hampp, Thorsten Fischer, Martin Neebe
Author Affiliations +
Proceedings Volume 4677, Optical Security and Counterfeit Deterrence Techniques IV; (2002) https://doi.org/10.1117/12.462703
Event: Electronic Imaging, 2002, San Jose, California, United States
Abstract
Bacteriorhodopsin is a two-dimensional crystalline photochromic protein which is astonishingly stable towards chemical and thermal degradation. This is one of the reasons why this is one of the very few proteins which may be used as a biological pigment in printing inks. Variants of the naturally occurring bacteriorhodopsin have been developed which show a distinguished color change even with low light intensities and without the requirement of UV-light. Several pigments with different color changes are available right now. In addition to this visual detectable feature, the photochromism, the proteins amino acid sequence can be genetically altered in order to code and identify specific production lots. For advanced applications the data storage capability of bacteriorhodopsin will be useful. Write-once-read-many (WORM) recording of digital data is accomplished by laser excitation of printed bacteriorhodopsin inks. A density of 1 MBit per square inch is currently achieved. Several application examples for this biological molecule are described where low and high level features are used in combination. Bacteriorhodopsin-based inks are a new class of optical security pigments.
© (2002) COPYRIGHT Society of Photo-Optical Instrumentation Engineers (SPIE). Downloading of the abstract is permitted for personal use only.
Norbert A. Hampp, Thorsten Fischer, and Martin Neebe "Bacteriorhodopsin-based photochromic pigments for optical security applications", Proc. SPIE 4677, Optical Security and Counterfeit Deterrence Techniques IV, (19 April 2002); https://doi.org/10.1117/12.462703
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Cited by 7 scholarly publications.
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KEYWORDS
Molecules

Polarization

Optical storage

Anisotropy

Data storage

Proteins

Crystals

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