Raman study of lysozyme amyloid fibrils suspended on super-hydrophobic surfaces by shear flow

被引:12
作者
Moretti, Manola [1 ,2 ,3 ]
Allione, Marco [1 ]
Marini, Monica [1 ]
Torre, Bruno [1 ]
Giugni, Andrea [1 ]
Limongi, Tania [1 ]
Das, Gobind [1 ]
Di Fabrizio, Enzo [1 ,4 ]
机构
[1] King Abdullah Univ Sci & Technol, Phys Sci & Engn, Thuwal 239556900, Saudi Arabia
[2] King Abdullah Univ Sci & Technol, Biol Div, Thuwal 239556900, Saudi Arabia
[3] King Abdullah Univ Sci & Technol, Environm Sci & Engn Div BESE, Thuwal 239556900, Saudi Arabia
[4] Univ Magna Graecia Viale Europa, Bionanotechnol & Engn Med BIONEM, Dept Expt & Clin Med, I-88100 Catanzaro, Italy
关键词
Super-hydrophobic micro-patterned surfaces; Raman spectroscopy; Amyloid fibrils; beta-sheet secondary structure; SECONDARY STRUCTURE; SPECTROSCOPY; PROTEINS; ORGANIZATION; AGGREGATION; PEPTIDES;
D O I
10.1016/j.mee.2017.05.045
中图分类号
TM [电工技术]; TN [电子技术、通信技术];
学科分类号
0808 ; 0809 ;
摘要
The shear flow generated at the rim of a drop evaporating on a micro-fabricated super-hydrophobic surface has been used to suspend and orient single/few lysozyme amyloid fibrils between two pillars for substrate-free characterization. Micro Raman spectroscopy performed on extended fibers evidenced a shift of the Amide Iband main peak to the value attributed to beta-sheet secondary structure, characteristic of the amyloid fibers. In addition, given the orientation sensitivity of the anisotropic molecule, the Raman signal of the main secondary structure was nicely enhanced for a fiber alignment parallel to the polarization direction of the laser. The substrate-free sample generated by this suspending technique is suitable for other structural analysis methods, where fiber crystals are investigated. It could be further employed for generation of arrays and patterns in a controllable fashion, where bio-compatible material is needed. (C) 2017 Elsevier B.V. All rights reserved.
引用
收藏
页码:194 / 198
页数:5
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