FT-Raman spectroscopy as diagnostic tool of Congo red binding to amyloids

被引:11
作者
Iconomidou, VA
Chryssikos, GD
Gionis, V
Hoenger, A
Hamodrakas, SJ [1 ]
机构
[1] Univ Athens, Dept Cell Biol & Biophys, Athens 15701, Greece
[2] Natl Hellen Res Fdn, Inst Theoret & Phys Chem, GR-11635 Athens, Greece
[3] European Mol Biol Lab, D-69117 Heidelberg, Germany
关键词
silkmoth chorion proteins; amyloid fibrils; electron microscopy; FT-Raman spectroscopy; Congo red binding;
D O I
10.1002/bip.10344
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Chorion is the major component of silkmoth eggshell. More than 95% of its dry mass consists of the A and B families of low molecular weight structural proteins, which have remarkable mechanical and chemical properties protecting the oocyte and developing embryo from environmental hazards. We present data from FT-Raman spectroscopy of silkmoth chorion and amyloid-like fibrils formed from peptide analogues of chorion proteins, both unstained and stained by Congo red. The results show that FT-Raman spectroscopy is not a straightforward diagnostic tool for the specific interactions of Congo red with amyloids: a dilute aqueous solution of the Congo red dye at pH 5.5 and a thin solid film of the dye cast from this solution exhibit the same "diagnostic" Raman shifts relative to the neat Congo red dry powder as do amyloid fibrils formed from peptide analogues of chorion proteins stained by Congo red. An important consequence of this finding is that these shifts of the Raman active modes of Congo red are probably due to the formation of supramolecular dye aggregates in the presence of water. Therefore, this is not an appropriate diagnostic test for Congo red binding to amyloids. (C) 2003 Wiley Periodicals, Inc.
引用
收藏
页码:185 / 192
页数:8
相关论文
共 28 条
[1]   VIBRATIONAL ANALYSIS OF PEPTIDES, POLYPEPTIDES, AND PROTEINS - CHARACTERISTIC AMIDE BANDS OF BETA-TURNS [J].
BANDEKAR, J ;
KRIMM, S .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1979, 76 (02) :774-777
[2]   Laser-Raman and FT-IR spectroscopic studies of peptide-analogues of silkmoth chorion protein segments [J].
Benaki, DC ;
Aggeli, A ;
Chryssikos, GD ;
Yiannopoulos, YD ;
Kamitsos, EI ;
Brumley, E ;
Case, ST ;
Boden, N ;
Hamodrakas, SJ .
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, 1998, 23 (01) :49-59
[3]  
Carey P.R., 1982, BIOCH APPL RAMAN RES
[4]   A model for structure-dependent binding of Congo red to Alzheimer β-amyloid fibrils [J].
Carter, DB ;
Chou, KC .
NEUROBIOLOGY OF AGING, 1998, 19 (01) :37-40
[5]   Protein misfolding, evolution and disease [J].
Dobson, CM .
TRENDS IN BIOCHEMICAL SCIENCES, 1999, 24 (09) :329-332
[6]  
Frushour B. G., 1975, ADV INFRARED RAMAN S, P35
[7]  
Hamodrakas S.J., 1992, Results and Problems in Cell Differentiation, V19, P115
[8]   LASER RAMAN STUDIES OF PROTEIN CONFORMATION IN THE SILKMOTH CHORION [J].
HAMODRAKAS, SJ ;
ASHER, SA ;
MAZUR, GD ;
REGIER, JC ;
KAFATOS, FC .
BIOCHIMICA ET BIOPHYSICA ACTA, 1982, 703 (02) :216-222
[9]   X-RAY-DIFFRACTION STUDIES OF A SILKMOTH CHORION [J].
HAMODRAKAS, SJ ;
PAULSON, JR ;
RODAKIS, GC ;
KAFATOS, FC .
INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES, 1983, 5 (03) :149-153
[10]   SECONDARY STRUCTURE PREDICTIONS FOR SILKMOTH CHORION PROTEINS [J].
HAMODRAKAS, SJ ;
JONES, CW ;
KAFATOS, FC .
BIOCHIMICA ET BIOPHYSICA ACTA, 1982, 700 (01) :42-51