Amino Acids

, Volume 47, Issue 12, pp 2551–2560 | Cite as

Tyrosine- and tryptophan-coated gold nanoparticles inhibit amyloid aggregation of insulin

  • Kriti Dubey
  • Bibin G. Anand
  • Rahul Badhwar
  • Ganesh Bagler
  • P. N. Navya
  • Hemant Kumar Daima
  • Karunakar Kar
Original Article

Abstract

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.

Keywords

Amyloid aggregation Tryptophan Tyrosine Insulin Gold nanoparticles 

Abbreviation

CD

Circular dichroism

AuNPsTyr

Tyrosine-coated gold nanoparticles

AuNPsTrp

Tryptophan-coated gold nanoparticles

AgNPsTyr

Tyrosine-coated silver nanoparticles

Tm

Transition temperature

Notes

Acknowledgments

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).

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.

Supplementary material

726_2015_2046_MOESM1_ESM.pdf (1.7 mb)
Supplementary material 1 (PDF 1702 kb)

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Copyright information

© Springer-Verlag Wien 2015

Authors and Affiliations

  • Kriti Dubey
    • 1
  • Bibin G. Anand
    • 1
  • Rahul Badhwar
    • 1
  • Ganesh Bagler
    • 1
  • P. N. Navya
    • 2
  • Hemant Kumar Daima
    • 2
  • Karunakar Kar
    • 1
  1. 1.Department of BiologyIndian Institute of Technology JodhpurJodhpurIndia
  2. 2.Department of BiotechnologySiddaganga Institute of TechnologyTumkurIndia

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