Literature DB >> 17711309

Nonspecific protein adsorption at the single molecule level studied by atomic force microscopy.

Peter Schön1, Martin Görlich, Michiel J J Coenen, Hans A Heus, Sylvia Speller.   

Abstract

Liquid tapping atomic force microscopy was used to study the nonspecific adsorption of horse spleen ferritin at a bare gold surface at single molecule resolution. The majority of ferritin molecules adsorbed irreversible on gold surfaces in accordance with the random sequential adsorption (RSA) mechanism frequently used to describe irreversible adsorption processes. However, the time-resolved data also reveal events that go beyond the RSA model, i.e., lateral mobility and fragility of some molecules, resulting in desorption, chain formation, and subunit dissociation. Scanning effects of the AFM tip were observed, resulting in diminished protein coverage in the scanned area.

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Year:  2007        PMID: 17711309     DOI: 10.1021/la700236z

Source DB:  PubMed          Journal:  Langmuir        ISSN: 0743-7463            Impact factor:   3.882


  4 in total

1.  Single-molecule observation of protein adsorption onto an inorganic surface.

Authors:  David J Niedzwiecki; John Grazul; Liviu Movileanu
Journal:  J Am Chem Soc       Date:  2010-08-11       Impact factor: 15.419

2.  Application of advanced sampling and analysis methods to predict the structure of adsorbed protein on a material surface.

Authors:  Tigran M Abramyan; David L Hyde-Volpe; Steven J Stuart; Robert A Latour
Journal:  Biointerphases       Date:  2017-05-17       Impact factor: 2.456

3.  Monitoring protein adsorption with solid-state nanopores.

Authors:  David J Niedzwiecki; Liviu Movileanu
Journal:  J Vis Exp       Date:  2011-12-02       Impact factor: 1.355

4.  Preparation and Characterization of Covalently Binding of Rat Anti-human IgG Monolayer on Thiol-Modified Gold Surface.

Authors:  Zhengjian Lv; Jianhua Wang; Linhong Deng; Guoping Chen
Journal:  Nanoscale Res Lett       Date:  2009-09-16       Impact factor: 4.703

  4 in total

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