Eugenol prevents amyloid formation of proteins and inhibits amyloid-induced hemolysis

被引:55
作者
Dubey, Kriti [1 ]
Anand, Bibin G. [1 ]
Shekhawat, Dolat Singh [1 ]
Kar, Karunakar [1 ,2 ]
机构
[1] Indian Inst Technol Jodhpur, Dept Biol, Jodhpur 342011, Rajasthan, India
[2] Jawaharlal Nehru Univ, Sch Life Sci, New Delhi 110067, India
来源
SCIENTIFIC REPORTS | 2017年 / 7卷
关键词
ALPHA-SYNUCLEIN OLIGOMERS; FIBRIL FORMATION; GLOBULAR-PROTEINS; ODORANT-BINDING; AGGREGATION; INSULIN; FLUORESCENCE; CELLS; CYTOTOXICITY; COMPONENTS;
D O I
10.1038/srep40744
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
Eugenol has attracted considerable attention because of its potential for many pharmaceutical applications including anti-inflammatory, anti-tumorigenic and anti-oxidant properties. Here, we have investigated the effect of eugenol on amyloid formation of selected globular proteins. We find that both spontaneous and seed-induced aggregation processes of insulin and serum albumin (BSA) are significantly suppressed in the presence of eugenol. Isothermal titration calorimetric data predict a single binding site for eugenol-insulin complex confirming the affinity of eugenol for native soluble insulin species. We also find that eugenol suppresses amyloid-induced hemolysis. Our findings reveal the inherent ability of eugenol to stabilize native proteins and to delay the conversion of protein species of native conformation into beta-sheet assembled mature fibrils, which seems to be crucial for its inhibitory effect.
引用
收藏
页数:11
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[1]   Protein aggregation diseases: pathogenicity and therapeutic perspectives [J].
Aguzzi, Adriano ;
O'Connor, Tracy .
NATURE REVIEWS DRUG DISCOVERY, 2010, 9 (03) :237-248
[2]   Secondary structure of α-synuclein oligomers:: Characterization by Raman and atomic force microscopy [J].
Apetri, MM ;
Maiti, NC ;
Zagorski, MG ;
Carey, PR ;
Anderson, VE .
JOURNAL OF MOLECULAR BIOLOGY, 2006, 355 (01) :63-71
[3]   Investigation of three flavonoids binding to bovine serum albumin using molecular fluorescence technique [J].
Bi, Shuyun ;
Yan, Lili ;
Pang, Bo ;
Wang, Yu .
JOURNAL OF LUMINESCENCE, 2012, 132 (01) :132-140
[4]  
Chamani J., 2010, J LUMIN, V130, P9
[5]   Stepwise Organization of the β- Structure Identifies Key Regions Essential for the Propagation and Cytotoxicity of Insulin Amyloid Fibrils [J].
Chatani, Eri ;
Imamura, Hiroshi ;
Yamamoto, Naoki ;
Kato, Minoru .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2014, 289 (15) :10399-10410
[6]   Investigations on the interactions of 5-fluorouracil with bovine serum albumin: Optical spectroscopic and molecular modeling studies [J].
Chinnathambi, Shanmugavel ;
Velmurugan, Devadasan ;
Hanagata, Nobutaka ;
Aruna, Prakasa Rao ;
Ganesan, Singaravelu .
JOURNAL OF LUMINESCENCE, 2014, 151 :1-10
[7]   Amyloid formation by globular proteins under native conditions [J].
Chiti, Fabrizio ;
Dobson, Christopher M. .
NATURE CHEMICAL BIOLOGY, 2009, 5 (01) :15-22
[8]   Effects of eugenol on Na+ currents in rat dorsal root ganglion neurons [J].
Cho, Jeong Seon ;
Kim, Tae Hoon ;
Lim, Jae-Min ;
Song, Jin-Ho .
BRAIN RESEARCH, 2008, 1243 :53-62
[9]   INSULIN AS AN AMYLOID-FIBRIL PROTEIN AT SITES OF REPEATED INSULIN INJECTIONS IN A DIABETIC PATIENT [J].
DISCHE, FE ;
WERNSTEDT, C ;
WESTERMARK, GT ;
WESTERMARK, P ;
PEPYS, MB ;
RENNIE, JA ;
GILBEY, SG ;
WATKINS, PJ .
DIABETOLOGIA, 1988, 31 (03) :158-161
[10]   Tyrosine- and tryptophan-coated gold nanoparticles inhibit amyloid aggregation of insulin [J].
Dubey, Kriti ;
Anand, Bibin G. ;
Badhwar, Rahul ;
Bagler, Ganesh ;
Navya, P. N. ;
Daima, Hemant Kumar ;
Kar, Karunakar .
AMINO ACIDS, 2015, 47 (12) :2551-2560