Tyrosine- and tryptophan-coated gold nanoparticles inhibit amyloid aggregation of insulin
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Here, we have strategically synthesized stable gold (AuNPsTyr, AuNPsTrp) and silver (AgNPsTyr) nanoparticles which are surface functionalized with either tyrosine or tryptophan residues and have examined their potential to inhibit amyloid aggregation of insulin. Inhibition of both spontaneous and seed-induced aggregation of insulin was observed in the presence of AuNPsTyr, AgNPsTyr, and AuNPsTrp nanoparticles. These nanoparticles also triggered the disassembly of insulin amyloid fibrils. Surface functionalization of amino acids appears to be important for the inhibition effect since isolated tryptophan and tyrosine molecules did not prevent insulin aggregation. Bioinformatics analysis predicts involvement of tyrosine in H-bonding interactions mediated by its C=O, –NH2, and aromatic moiety. These results offer significant opportunities for developing nanoparticle-based therapeutics against diseases related to protein aggregation.
KeywordsAmyloid aggregation Tryptophan Tyrosine Insulin Gold nanoparticles
Tyrosine-coated gold nanoparticles
Tryptophan-coated gold nanoparticles
Tyrosine-coated silver nanoparticles
We thank IIT Jodhpur for research facilities. We thank IIT Bombay for use of the Cryo HR-TEM Central Facility. This work was supported by BRNS grant (KK) (Grant No.37(1)/14/38/2014-BRNS) and Seed Grant from Indian Institute of Technology Jodhpur (KK and GB). HKD gratefully acknowledges Department of Science and Technology (DST), Government of India for ITS Grant (Grant No. SB/ITS-Y/0988/2014-15).
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Conflict of interest
The authors declare that they have no conflict of interest.
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