Solid surface dependent layering of self-arranged structures with fibril-like assemblies of alpha-synuclein

被引:5
|
作者
Bukauskas, V. [1 ]
Setkus, A. [1 ]
Simkiene, I. [1 ]
Tumenas, S. [1 ]
Kasalynas, I. [1 ]
Reza, A. [1 ]
Babonas, J. [1 ]
Casaite, V. [2 ]
Poviloniene, S. [2 ]
Meskys, R. [2 ]
机构
[1] Ctr Phys Sci & Technol, LT-01108 Vilnius, Lithuania
[2] Vilnius Univ, Inst Biochem, LT-08662 Vilnius, Lithuania
关键词
Biomolecular structures; Scanning probe microscopy; Optical properties; VIBRATIONAL CIRCULAR-DICHROISM; PEPTIDE SECONDARY STRUCTURE; ATOMIC-FORCE MICROSCOPY; CONFORMATIONAL DETERMINATION; PARKINSONS-DISEASE; PROTEIN; SPECTROSCOPY; AGGREGATION; SPECTRA; MODEL;
D O I
10.1016/j.apsusc.2011.12.120
中图分类号
O64 [物理化学(理论化学)、化学物理学];
学科分类号
070304 ; 081704 ;
摘要
In present work the formation of hybrid constructions composed of alpha-synuclein-based colloidal solutions on various solid surfaces (silica coated Si, mica, CaF2 and KBr) is investigated by scanning probe microscopy, spectrocopic ellipsometry, Fourier transformed infrared spectroscopy and vibrational circular dichroism. Prior to the modification of the solids, the proteins were intentionally fibrilled under special conditions. It is proved that the multi-component coatings are self-arranged on the solid substrates. Depending on the substrate material, the interface films consisting of individual biomolecules can be detected on the solid surfaces. The coatings with fibril-like alpha-synuclein objects can be obtained on solid surfaces with negligible or comparatively thick interface films. The results are interpreted in terms of the charged surface-controlled electrostatic interaction between the substrate and the biomolecules. Solubility of solids is considered in this interpretation. (C) 2012 Elsevier B.V. All rights reserved.
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页码:4383 / 4390
页数:8
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