scholarly journals PEGylated surfaces for the study of DNA–protein interactions by atomic force microscopy

Nanoscale ◽  
2019 ◽  
Vol 11 (42) ◽  
pp. 20072-20080
Author(s):  
Bernice Akpinar ◽  
Philip J. Haynes ◽  
Nicholas A. W. Bell ◽  
Katharina Brunner ◽  
Alice L. B. Pyne ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Protein Interactions ◽  
Polymer Surfaces ◽  
Block Polymer ◽  
Force Microscopy ◽  
Atomic Force ◽  
Dna Protein Interactions

Co-block polymer surfaces provide a platform on which to visualize DNA–protein interactions by atomic force microscopy at nanometre resolution.

Specific DNA−Protein Interactions on Mica Investigated by Atomic Force Microscopy

Langmuir ◽  
2010 ◽  
Vol 26 (4) ◽  
pp. 2618-2623 ◽  
Author(s):  
David Pastré ◽  
Loïc Hamon ◽  
Isabelle Sorel ◽  
Eric Le Cam ◽  
Patrick A. Curmi ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Protein Interactions ◽  
Force Microscopy ◽  
Atomic Force ◽  
Dna Protein Interactions

Dynamic imaging of single DNA–protein interactions using atomic force microscopy

2003 ◽  
Vol 479 (1) ◽  
pp. 3-15 ◽  
Author(s):  
Martin L. Bennink ◽  
Dessy N. Nikova ◽  
Kees O. van der Werf ◽  
Jan Greve
Keyword(s):  
Atomic Force Microscopy ◽  
Protein Interactions ◽  
Dynamic Imaging ◽  
Force Microscopy ◽  
Atomic Force ◽  
Dna Protein Interactions

scholarly journals PEGylated surfaces for the study of DNA-protein interactions by atomic force microscopy

2019 ◽  
Author(s):  
Bernice Akpinar ◽  
Nicholas A. W. Bell ◽  
Alice L.B. Pyne ◽  
Bart W. Hoogenboom
Keyword(s):  
Atomic Force Microscopy ◽  
Block Copolymers ◽  
Protein Interactions ◽  
Selective Adsorption ◽  
Regulation Of Gene Expression ◽  
Relevant Information ◽  
Solid Substrate ◽  
Force Microscopy ◽  
Atomic Force ◽  
Dna Protein Interactions

AbstractDNA-protein interactions are vital to cellular function, with key roles in the regulation of gene expression and genome maintenance. Atomic force microscopy (AFM) offers the ability to visualize DNA-protein interactions at nanometre resolution in near-physiological buffers, but it requires that the DNA be adhered to the surface of a solid substrate. This presents a problem when working at biologically relevant protein concentrations, where protein may be present at large excess in solution; much of the biophysically relevant information can therefore be occluded by non-specific protein binding to the underlying substrate. Here we explore the use of PLLx-b-PEGy block copolymers to achieve selective adsorption of DNA on a mica surface. Through varying both the number of lysine and ethylene glycol residues in the block copolymers, we show selective adsorption of DNA on mica that is functionalized with a PLL10-b-PEG113 / PLL1000-2000 mixture as viewed by AFM imaging in a solution containing high concentrations of streptavidin. We show that this selective adsorption extends to DNA-protein complexes, through the use of biotinylated DNA and streptavidin, and demonstrate that DNA-bound streptavidin can be unambiguously distinguished by in-liquid AFM in spite of an excess of unbound streptavidin in solution.

scholarly journals Substrate Chemistry-Dependent Conformations of Single Laminin Molecules on Polymer Surfaces are Revealed by the Phase Signal of Atomic Force Microscopy

2007 ◽  
Vol 93 (1) ◽  
pp. 202-207 ◽  
Author(s):  
Jose Carlos Rodríguez Hernández ◽  
Manuel Salmerón Sánchez ◽  
José Miguel Soria ◽  
José Luis Gómez Ribelles ◽  
Manuel Monleón Pradas
Keyword(s):  
Atomic Force Microscopy ◽  
Polymer Surfaces ◽  
Force Microscopy ◽  
Atomic Force ◽  
Phase Signal

scholarly journals Optical switching of protein interactions on photosensitive–electroactive polymers measured by atomic force microscopy

2013 ◽  
Vol 1 (16) ◽  
pp. 2162 ◽  
Author(s):  
Amy Gelmi ◽  
Michele Zanoni ◽  
Michael J. Higgins ◽  
Sanjeev Gambhir ◽  
David L. Officer ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Protein Interactions ◽  
Optical Switching ◽  
Electroactive Polymers ◽  
Force Microscopy ◽  
Atomic Force
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