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Albisetti E, Carroll KM, Lu X, et al. Thermochemical scanning probe lithography of protein gradients at the nanoscale. Nanotechnology. 2016;27(31):315302doi: 10.1088/0957-4484/27/31/315302.
Albisetti, E., Carroll, K. M., Lu, X., Curtis, J. E., Petti, D., Bertacco, R., & Riedo, E. (2016). Thermochemical scanning probe lithography of protein gradients at the nanoscale. Nanotechnology, 27(31), 315302. https://doi.org/10.1088/0957-4484/27/31/315302
Albisetti, E, et al. "Thermochemical scanning probe lithography of protein gradients at the nanoscale." Nanotechnology vol. 27,31 (2016): 315302. doi: https://doi.org/10.1088/0957-4484/27/31/315302
Albisetti E, Carroll KM, Lu X, Curtis JE, Petti D, Bertacco R, Riedo E. Thermochemical scanning probe lithography of protein gradients at the nanoscale. Nanotechnology. 2016 Aug 05;27(31):315302. doi: 10.1088/0957-4484/27/31/315302. Epub 2016 Jun 27. PMID: 27344982.
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Nanotechnology. 2016 Aug 05;27(31):315302. doi: 10.1088/0957-4484/27/31/315302. Epub 2016 Jun 27.

Thermochemical scanning probe lithography of protein gradients at the nanoscale.

Nanotechnology

E Albisetti, K M Carroll, X Lu, J E Curtis, D Petti, R Bertacco, E Riedo

Affiliations

  1. Dipartimento di Fisica, Politecnico di Milano, 20133 Milano, Italy. School of Physics, Georgia Institute of Technology, Atlanta, GA 30332, USA.

PMID: 27344982 DOI: 10.1088/0957-4484/27/31/315302

Abstract

Patterning nanoscale protein gradients is crucial for studying a variety of cellular processes in vitro. Despite the recent development in nano-fabrication technology, combining nanometric resolution and fine control of protein concentrations is still an open challenge. Here, we demonstrate the use of thermochemical scanning probe lithography (tc-SPL) for defining micro- and nano-sized patterns with precisely controlled protein concentration. First, tc-SPL is performed by scanning a heatable atomic force microscopy tip on a polymeric substrate, for locally exposing reactive amino groups on the surface, then the substrate is functionalized with streptavidin and laminin proteins. We show, by fluorescence microscopy on the patterned gradients, that it is possible to precisely tune the concentration of the immobilized proteins by varying the patterning parameters during tc-SPL. This paves the way to the use of tc-SPL for defining protein gradients at the nanoscale, to be used as chemical cues e.g. for studying and regulating cellular processes in vitro.

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