Tyrosine-Generated Nanostructures Initiate Amyloid Cross-Seeding in Proteins Leading to a Lethal Aggregation Trap

被引:36
作者
Anand, Bibin G. [1 ,2 ]
Prajapati, Kailash P. [1 ]
Shekhawat, Dolat S. [1 ,3 ]
Kar, Karunakar [1 ]
机构
[1] Jawaharlal Nehru Univ, Sch Life Sci, Biophys & Biomat Res Lab, Room 310, New Delhi 110067, India
[2] Univ Alberta, Dept Med, Edmonton, AB T6G 2G3, Canada
[3] All India Inst Med Sci, Dept Pediat, Jodhpu, Rajasthan, India
关键词
GOLD NANOPARTICLES; L-PHENYLALANINE; FIBRILS; PHENYLKETONURIA; COAGGREGATION; INHIBITION; ASSEMBLIES; INSIGHT; MODEL;
D O I
10.1021/acs.biochem.8b00472
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
Here, we show that aromatic amino acid tyrosine, under a physiologically mimicking condition, readily forms amyloid-like entities that can effectively drive aggregation of different globular proteins and aromatic residues. Tyrosine self assembly resulted in the formation of cross-beta rich regular fibrils as well as spheroidal oligomers. Computational data suggest intermolecular interaction between specifically oriented tyrosine molecules mediated through pi-pi stacking and H-bonding interactions, mimicking a cross-beta-like architecture. Both individual protein samples and mixed protein samples underwent aggregation in the presence of tyrosine fibrils, confirming the occurrence of amyloid cross-seeding. The surface of the tyrosine's amyloid like entities was predicted to trap native protein structures, preferably through hydrophobic and electrostatic interactions initiating an aggregation event. Because tyrosine is a precursor to vital neuromodulators, the inherent cross-seeding potential of the tyrosine fibrils may have direct relevance to amyloid-linked pathologies.
引用
收藏
页码:5202 / 5209
页数:8
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