Literature DB >> 25535923

Following the aggregation of human prion protein on Au(111) surface in real-time.

Bin Wang1, Cunlan Guo, Zhichao Lou, Bingqian Xu.   

Abstract

Aggregations of human prion protein (23-231) were monitored by atomic force microscopy in real-time under pH 4. Prion dimers and trimers were determined as the basic units by AFM images and simulated structures. Aggregates aligned with the herringbone structures of an Au(111) reconstructed surface via Au-S bonds as the first layer, while the second layer was formed by non-covalent interactions.

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Year:  2014        PMID： 25535923     DOI： 10.1039/c4cc09209k

Source DB:  PubMed          Journal:  Chem Commun (Camb)        ISSN： 1359-7345            Impact factor:   6.222


  3 in total

1.  Qualitative and Quantitative Detection of PrPSc Based on the Controlled Release Property of Magnetic Microspheres Using Surface Plasmon Resonance (SPR).

Authors:  Zhichao Lou; He Han; Dun Mao; Yibin Jiang; Jianyue Song
Journal:  Nanomaterials (Basel)       Date:  2018-02-13       Impact factor: 5.076

2.  Direct observation of prion protein oligomer formation reveals an aggregation mechanism with multiple conformationally distinct species.

Authors:  Jason C Sang; Ji-Eun Lee; Alexander J Dear; Suman De; Georg Meisl; Alana M Thackray; Raymond Bujdoso; Tuomas P J Knowles; David Klenerman
Journal:  Chem Sci       Date:  2019-03-25       Impact factor: 9.825

3.  BODIPY-Based Fluorescent Probes for Sensing Protein Surface-Hydrophobicity.

Authors:  Nethaniah Dorh; Shilei Zhu; Kamal B Dhungana; Ranjit Pati; Fen-Tair Luo; Haiying Liu; Ashutosh Tiwari
Journal:  Sci Rep       Date:  2015-12-18       Impact factor: 4.379
  3 in total

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