Nanomedicine: Nanotechnology, Biology and Medicine
Volume 5, Issue 1 , Pages 21-29 , March 2009

Anti-glycation activity of gold nanoparticles

  • Santiswarup Singha, MSc

      Affiliations

    • Department of Biochemistry, Calcutta University, Kolkata, India
  • ,
  • Jaydeep Bhattacharya, PhD

      Affiliations

    • Department of Biochemistry, Calcutta University, Kolkata, India
  • ,
  • Himadri Datta, MS, PhD

      Affiliations

    • Regional Institute of Ophthalmology, Calcutta Medical College, Kolkata, India
  • ,
  • Anjan Kumar Dasgupta, PhD

      Affiliations

    • Department of Biochemistry, Calcutta University, Kolkata, India
    • Corresponding Author InformationCorresponding author. Calcutta University, Kolkata, WB 700019, India.

Received 11 March 2008 ,Accepted 7 June 2008.

References 

  1. Ingolia TD, Craig EA. Four small Drosophila heat shock proteins are related to each other and to mammalian alpha-crystallin. Proc Natl Acad Sci U S A. 1982;79:2360–2364
  2. Xia JZ, Wang Q, Tatarkova S, Aerts T, Clauwaert J. Structural basis of eye lens transparency: light scattering by concentrated solutions of bovine α-crystallin proteins. Biophys J. 1996;71:2815–2822
  3. Carver JA, Aquilina JA, Truscott RJ. An investigation into the stability of alpha-crystallin by NMR spectroscopy; evidence for a two-domain structure. Biochim Biophys Acta. 1993;1164:22–28
  4. Fujii N, Nakamura T, Sadakane Y, Saito T, Fujii N. Differential susceptibility of alpha A- and alpha B-crystallin to gamma-ray irradiation. Biochim Biophys Acta. 2007;1774:345–350
  5. Peterson JJ, Young MM, Takemoto LJ. Probing alpha-crystallin structure using chemical cross-linkers and mass spectrometry. Mol Vis. 2004;10:857–866
  6. Augusteyn RC, Stevens A. Macromolecular structure of the eye lens. Prog Polym Sci. 1998;23:375–413
  7. Haslbeck M, Walke S, Stromer T, Ehrnsperger M, White HE, Chen S, et al. Hsp26: a temperature-regulated chaperone. EMBO J. 1999;18:6744–6751
  8. van den Oetelaar PJ, van Someren PF, Thomson JA, Siezen RJ, Hoenders HJ. A dynamic quaternary structure of bovine alpha-crystallin as indicated from intermolecular exchange of subunits. Biochemistry. 1990;29:3488–3493
  9. Das KP, Surewicz WK. Temperature-induced exposure of hydrophobic surfaces and its effect on the chaperone activity of alpha-crystallin. FEBS Lett. 1995;369:321–325
  10. Bhattacharyya J, Shipova EV, Santhoshkumar P, Sharma KK, Ortwerth BJ. Effect of a Single AGE modification on the structure and chaperone activity of human alpha B-crystallin. Biochemistry. 2007;46:14682–14692
  11. GhoshMoulick R, Bhattacharya J, Roy S, Basak S, Dasgupta AK. Compensatory secondary structure alterations in protein glycation. Biochim Biophys Acta. 2007;1774:233–242
  12. GhoshMoulick R, Bhattacharya J, Mitra CK, Basak S, Dasgupta AK. Protein seeding of gold nanoparticles and mechanism of glycation sensing. Nanomedicine. 2007;3:208–214
  13. Roy S, Dasgupta AK. Controllable self-assembly from fibrinogen-gold (fibrinogen-Au) and thrombin-silver (thrombin-Ag) nanoparticle interaction. FEBS Lett. 2007;581:5533–5542
  14. Saha B, Bhattacharya J, Mukherjee A, Ghosh AK, Santra CR, Dasgupta AK, et al. In vitro structural and functional evaluation of gold nanoparticles conjugated antibiotics. Nanoscale Res Lett. 2007;2:614–622
  15. Bhattacharya J, Jasrapuria S, Sarkar T, GhoshMoulick R, Dasgupta AK. Gold nanoparticle based tool to study protein conformational variants: implications in hemoglobinopathy. Nanomedicine. 2007;3:14–19
  16. Roy S, Singha S, Bhattacharya J, GhoshMoulick R, Dasgupta AK. A size dependent folding contour for cytochrome c. Biophys Chem. 2006;119:15–23
  17. Kumar PA, Suryanarayana P, Reddy PY, Reddy GB. Modulation of alpha-crystallin chaperone activity in diabetic rat lens by curcumin. Mol Vis. 2005;11:561–568
  18. Carver JA, Aquilina JA, Truscott RJ. A possible chaperone-like quaternary structure for alpha-crystallin. Exp Eye Res. 1994;59:231–234
  19. Augusteyn RC. Alpha-crystallin: a review of its structure and function. Clin Exp Optom. 2004;87:356–366
  20. Sastry M, Kumar A, Datar S, Dharmadhikari CV, Ganesh KN. DNA-mediated electrostatic assembly of gold nanoparticles into linear arrays by a simple drop-coating procedure. Appl Phys Lett. 2001;78:2943
  21. Hu X, Cheng W, Wang T, Wang E, Dong S. Well-ordered end-to-end linkage of gold nanorods. Nanotechnology. 2005;16:2164–2169
  22. Hipkiss AR. Carnosine and protein carbonyl groups: a possible relationship. Biochemistry. 2000;65:771–778

 Sources of support include Grant No. BT/PR9953/MNT/28/73/2007, Department of Biotechnology (DBT), Government of India.

PII: S1549-9634(08)00090-7

doi: 10.1016/j.nano.2008.06.005

Nanomedicine: Nanotechnology, Biology and Medicine
Volume 5, Issue 1 , Pages 21-29 , March 2009