Micrometer sized immobilization of protein molecules onto quartz, silicium and gold.

Steffen B. Petersen; Maria Teresa Neves-Petersen; Søren Klitgaard; Meg Crookshanks Duroux

doi:10.1117/12.664086

13 February 2006 Micrometer sized immobilization of protein molecules onto quartz, silicium and gold.

Steffen B. Petersen, Maria Teresa Neves-Petersen, Søren Klitgaard, Meg Crookshanks Duroux

Proceedings Volume 6106, Photon Processing in Microelectronics and Photonics V; 61061Y (2006) https://doi.org/10.1117/12.664086
Event: Lasers and Applications in Science and Engineering, 2006, San Jose, California, United States

Abstract

We demonstrate that ultraviolet light can be used to make sterically oriented covalent immobilization of a large variety of protein molecules onto either gold or thiolated quartz or silicium. The reaction mechanism behind the reported new technology involves light induced breakage of disulphide bridges in proteins upon UV illumination of nearby aromatic amino acids, resulting in the formation of free, reactive thiol groups that will form covalent bonds with thiol reactive surfaces. The protein molecules in general retain their function. The size of the immobilization spot is determined by the dimension of the UV beam. In principle, the spot size may be as small as 1 micrometer or less. We have developed the necessary technology for preparing large protein arrays of enzymes and fragments of monoclonal antibodies. Dedicated Image Processing Software has been developed for making quality assessment of the protein arrays. A multitude of important application areas such as drug carriers and drug delivery, bioelectronics, carbon nanotubes, nanoparticles as well as protein glue are discussed.

Citation Download Citation

Steffen B. Petersen, Maria Teresa Neves-Petersen, Søren Klitgaard, and Meg Crookshanks Duroux "Micrometer sized immobilization of protein molecules onto quartz, silicium and gold.", Proc. SPIE 6106, Photon Processing in Microelectronics and Photonics V, 61061Y (13 February 2006); https://doi.org/10.1117/12.664086

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