Nano-patterned SERS substrate: Application for protein analysis vs. temperature

被引:211
作者
Das, Gobind [1 ,2 ]
Mecarini, Federico [1 ,2 ]
Gentile, Francesco [1 ,2 ]
De Angelis, Francesco [1 ,2 ]
Kumar, Mohan H. G. [3 ]
Candeloro, Patrizio [1 ]
Liberale, Carlo [1 ,2 ]
Cuda, Giovanni [2 ,3 ]
Di Fabrizio, Enzo [1 ,2 ,4 ]
机构
[1] Magna Graecia Univ Catanzaro, Dipartimento Med Sperimentale & Clin, Lab BIONEM, Catanzaro, Italy
[2] CalMED Srl, Sede Catanzaro Cda Mula Loc Germaneto, I-88100 Catanzaro, Italy
[3] Magna Graecia Univ Catanzaro, Dipartimento Med Sperimentale & Clin, Prote Lab, Catanzaro, Italy
[4] INFM TASC SS, Basovizza Trieste, Italy
关键词
SERS; Proteins; Difference and 2D-correlation Raman spectroscopy; Temperature variation; RESONANCE RAMAN-SPECTROSCOPY; VIRUS STRUCTURE; CONFORMATION; DIFFERENCE; SCATTERING; STABILITY; LYSOZYME; SPECTRA; ACID;
D O I
10.1016/j.bios.2008.08.050
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
We have illustrated the fabrication of nano-structures as a surface enhanced Raman scattering (SERS) substrate using electro-plating and electron-beam lithography techniques to obtain an array of gold nanograin-aggregate structures of diameter ranging between 80 and 100nm with interstitial gap of 10-30 nm. The nanostructure based SERS substrate permits us to have better control and reproducibility on generation of plasmon polaritons. The calculation shows the possible detection of myoglobin concentration down to attomole. This SERS substrate is used to investigate the structural changes of different proteins; lysozyme, ribonuclease-B, bovin serum albumin and myoglobin in the temperature range between -65 and 90 degrees C. The in-depth analysis even for small conformational changes is performed using 2D Raman correlation analysis and difference Raman analysis in order to gain straightforward understanding of proteins undergoing thermodynamical perturbation. (C) 2008 Elsevier B.V. All rights reserved.
引用
收藏
页码:1693 / 1699
页数:7
相关论文
共 36 条
[1]   THE STRUCTURES OF THE MONOCLINIC AND ORTHORHOMBIC FORMS OF HEN EGG-WHITE LYSOZYME AT 6-A RESOLUTION [J].
ARTYMIUK, PJ ;
BLAKE, CCF ;
RICE, DW ;
WILSON, KS .
ACTA CRYSTALLOGRAPHICA SECTION B-STRUCTURAL SCIENCE, 1982, 38 (MAR) :778-783
[2]   Protein stability induced by ligand binding correlates with changes in protein flexibility [J].
Celej, MS ;
Montich, CG ;
Fidelio, GD .
PROTEIN SCIENCE, 2003, 12 (07) :1496-1506
[3]  
[陈建华 CHEN Jianhua], 2006, [中国药科大学学报, Journal of China Pharmaceutical University], V37, P277
[4]   UV resonance Raman-selective amide vibrational enhancement: Quantitative methodology for determining protein secondary structure [J].
Chi, ZH ;
Chen, XG ;
Holtz, JSW ;
Asher, SA .
BIOCHEMISTRY, 1998, 37 (09) :2854-2864
[5]   Single-molecule detection using surface-enhanced resonance Raman scattering and Langmuir-Blodgett monolayers [J].
Constantino, CJL ;
Lemma, T ;
Antunes, PA ;
Aroca, R .
ANALYTICAL CHEMISTRY, 2001, 73 (15) :3674-3678
[6]   Study of the ribonuclease S-peptide/S-protein complex by means of Raman difference spectroscopy [J].
Gilmanshin, R ;
VanBeek, J ;
Callender, R .
JOURNAL OF PHYSICAL CHEMISTRY, 1996, 100 (41) :16754-16760
[7]   Stability of helix-rich proteins at high concentrations [J].
Guo, Jianxin ;
Harn, Nicholas ;
Robbins, Aaron ;
Dougherty, Ron ;
Middaugh, C. Russell .
BIOCHEMISTRY, 2006, 45 (28) :8686-8696
[8]   Solution-phase, triangular Ag nanotriangles fabricated by nanosphere lithography [J].
Haes, AJ ;
Zhao, J ;
Zou, SL ;
Own, CS ;
Marks, LD ;
Schatz, GC ;
Van Duyne, RP .
JOURNAL OF PHYSICAL CHEMISTRY B, 2005, 109 (22) :11158-11162
[9]   Surface-enhanced Raman spectroscopy [J].
Haynes, CL ;
McFarland, AD ;
Van Duyne, RP .
ANALYTICAL CHEMISTRY, 2005, 77 (17) :338A-346A
[10]   SURFACE-ENHANCED RESONANCE RAMAN-SPECTROSCOPY OF RHODAMINE-6G ADSORBED ON COLLOIDAL SILVER [J].
HILDEBRANDT, P ;
STOCKBURGER, M .
JOURNAL OF PHYSICAL CHEMISTRY, 1984, 88 (24) :5935-5944