Skip to main content
SpringerLink
Log in

The Interactions of Glutathione-Capped CdTe Quantum Dots with Trypsin

  • Published:
Biological Trace Element Research Aims and scope Submit manuscript

Abstract

Due to their unique fluorescent properties, quantum dots present a great potential for biolabelling applications; however, the toxic interactions of quantum dots with biopolymers are little known. The toxic interactions of glutathione-capped CdTe quantum dots with trypsin were studied in this paper using synchronous fluorescence spectroscopy, fluorescence emission spectra, and UV–vis absorption spectra. The interaction between CdTe quantum dots and trypsin resulted in structure changes of trypsin and inhibited trypsin's activity. Fluorescence emission spectra revealed that the quenching mechanism of trypsin by CdTe quantum dots was a static quenching process. The binding constant and the number of binding sites at 288 and 298 K were calculated to be 1.98 × 106 L mol−1 and 1.37, and 6.43 × 104 L mol−1 and 1.09, respectively. Hydrogen bonds and van der Waals' forces played major roles in this process.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

Scheme 1
Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5
Fig. 6

Similar content being viewed by others

References

  1. Weng JF, Song XT, Li LA et al (2006) Highly luminescent CdTe quantum dots prepared in aqueous phase as an alternative fluorescent probe for cell imaging. Talanta 2:397–402

    Article  Google Scholar 

  2. Medintz IL, Uyeda HT, Goldman ER et al (2005) Quantum dot bioconjugates for imaging, labelling and sensing. Nat Mater 6:435–446

    Article  Google Scholar 

  3. Jamieson T, Bakhshi R, Petrova D et al (2007) Biological applications of quantum dots. Biomaterials 31:4717–4732

    Article  Google Scholar 

  4. Rehberg M, Praetner M, Leite CF et al (2010) Quantum dots modulate leukocyte adhesion and transmigration depending on their surface modification. Nano Lett 9:3656–3664

    Article  Google Scholar 

  5. Shiohara A, Hoshino A, Hanaki K et al (2004) On the cyto-toxicity caused by quantum dots. Microbiol Immunol 9:669–675

    Google Scholar 

  6. Lovric J, Bazzi HS, Cuie Y et al (2005) Differences in subcellular distribution and toxicity of green and red emitting CdTe quantum dots. J Mol Med-Jmm 5:377–385

    Article  Google Scholar 

  7. Hardman R (2006) A toxicologic review of quantum dots: toxicity depends on physicochemical and environmental factors. Environ Health Persp 2:165–172

    Article  Google Scholar 

  8. Zhao LZ, Liu RT, Zhao XC et al (2009) New strategy for the evaluation of CdTe quantum dot toxicity targeted to bovine serum albumin. Sci Total Environ 18:5019–5023

    Google Scholar 

  9. Ghosh S, Banerjee A (2002) A multitechnique approach in protein/surfactant interaction study: physicochemical aspects of sodium dodecyl sulfate in the presence of trypsin in aqueous medium. Biomacromolecules 1:9–16

    Article  Google Scholar 

  10. Huang YB, Liu BZ, Yu Z et al (2010) Luminescence quenching effect for the interaction of prulifloxacin with trypsin-Britton-Robinson buffer solution system. J Lumin 3:360–364

    Article  Google Scholar 

  11. Zhang HM, Zhou QH, Wang YQ (2010) Studies on the interactions of 2, 4-dinitrophenol and 2, 4-dichlorphenol with trypsin. J Fluoresc 2:507–516

    Article  Google Scholar 

  12. Jingzhou F (2010) Multi–spectroscopic study on the interaction between CdTe quantum dots and bovine serum albumin. Chin J Chem 28:2353–2358

    Article  Google Scholar 

  13. Shi L, Rosenzweig N, Rosenzweig Z (2007) Luminescent quantum dots fluorescence resonance energy transfer-based probes for enzymatic activity and enzyme inhibitors. Anal Chem 1:208–214

    Article  Google Scholar 

  14. Blanco-Canosa JB, Medintz IL, Farrell D et al (2010) Rapid covalent ligation of fluorescent peptides to water solubilized quantum dots. J Am Chem Soc 29:10027–10033

    Article  Google Scholar 

  15. Wang L, Gong HB, Lv RJ et al (2010) A one-pot aqueous synthesis of high-luminescent thiol-capped CdTe and its bioapplication. J Nanosci Nanotechnol 10:1–5

    Article  Google Scholar 

  16. Schwert GW, Takenaka Y (1955) A spectrophotometric determination of trypsin and chymotrypsin. Biochim Biophys Acta 16:570–575

    Article  PubMed  CAS  Google Scholar 

  17. Stellmach B (1988) Trypsin. In: Qian JY (ed) The methods of enzyme activity determination, Chinese edition. China Light Industry Press, Beijing

  18. Marrakchi M, Dzyadevych SV, Biloivan OA et al (2006) Development of trypsin biosensor based on ion sensitive field-effect transistors for proteins determination. Mat Sci Eng C-Bio Syst 2–3:369–373

    Article  Google Scholar 

  19. Koutsopoulos S, Patzsch K, Bosker WTE et al (2007) Adsorption of trypsin on hydrophilic and hydrophobic surfaces. Langmuir 4:2000–2006

    Article  Google Scholar 

  20. Bowen S, Hilty C (2008) Time-resolved dynamic nuclear polarization enhanced NMR spectroscopy. Angew Chem Int Edit 28:5235–5237

    Google Scholar 

  21. Yu YQ, Gilar M, Lee PJ et al (2003) Enzyme-friendly, mass spectrometry-compatible surfactant for in-solution enzymatic digestion of proteins. Anal Chem 21:6023–6028

    Article  Google Scholar 

  22. Zhao XC, Liu RT, Chi ZX et al (2010) New insights into the behavior of bovine serum albumin adsorbed onto carbon nanotubes: comprehensive spectroscopic studies. J Phys Chem B 16:5625–5631

    Article  Google Scholar 

  23. Rk S (1974) Measurement of protein by spectrophotometry at 205 nm. Anal Biochem 1:277–282

    Google Scholar 

  24. Aitken A, Learmonth M (1996) Protein determination by UV absorption. In: Walker JM (ed) The protein protocols handbook, 2nd edn. Humana Press Inc., Totowa, pp 3–6

    Chapter  Google Scholar 

  25. Beaven GH, Holiday ER (1952) Ultraviolet absorption spectra of proteins and amino acids. Adv Protein Chem 7:319–386

    Article  PubMed  CAS  Google Scholar 

  26. Edelhoch H (1967) Spectroscopic determination of tryptophan and tyrosine in proteins. Biochem 7:1948–1954

    Google Scholar 

  27. Pace CN, Vajdos F, Fee L et al (1995) How to measure and predict the molar absorption coefficient of a protein. Prot Sci 11:2411–2423

    Article  Google Scholar 

  28. Chi ZX, Liu RT, Zhang H (2010) Noncovalent interaction of oxytetracycline with the enzyme trypsin. Biomacromolecules 9:2454–2459

    Article  Google Scholar 

  29. Zhang YZ, Zhou B, Liu YX et al (2008) Fluorescence study on the interaction of bovine serum albumin with p-aminoazobenzene. J Fluoresc 1:109–118

    Article  Google Scholar 

  30. Zhang HM, Wang YQ, Zhou QH (2009) Investigation of the interactions of quercetin and morin with trypsin. Luminescence 5:355–362

    Article  Google Scholar 

  31. Hu YJ, Liu Y, Wang HB et al (2004) Study of the interaction between monoammonium glycyrrhizinate and bovine serum albumin. J Pharmaceut Biomed 4:915–919

    Article  Google Scholar 

  32. Gong AQ, Zhu XS, Hu YY et al (2007) A fluorescence spectroscopic study of the interaction between epristeride and bovin serum albumine and its analytical application. Talanta 4:668–673

    Article  Google Scholar 

  33. Soragni A, Zambelli B, Mukrasch MD et al (2008) Structural characterization of binding of Cu(II) to Tau protein. Biochemistry 41:10841–10851

    Article  Google Scholar 

  34. Ross PD, Subramanian S (1981) Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry 11:3096–3102

    Article  Google Scholar 

Download references

Acknowledgments

This work is supported by NSFC (20875055), the Cultivation Fund of the Key Scientific and Technical Innovation Project, and the Ministry of Education of China (708058), and the Key Science-Technology Project in Shandong Province (2008GG10006012) is also acknowledged.

Author information

Authors and Affiliations

  1. Shandong Key Laboratory of Water Pollution Control and Resource Reuse, School of Environmental Science and Engineering Shandong University, China–America CRC for Environment & Health, Shandong Province, 27# Shanda South Road, Jinan, 250100, People’s Republic of China

    Bingjun Yang & Rutao Liu

  2. State Key Laboratory of Crystal Materials, Shandong University, Jinan, 250100, People’s Republic of China

    Xiaopeng Hao, Yongzhong Wu & Jie Du

Authors
  1. Bingjun Yang
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Rutao Liu
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Xiaopeng Hao
    View author publications

    You can also search for this author in PubMed Google Scholar

  4. Yongzhong Wu
    View author publications

    You can also search for this author in PubMed Google Scholar

  5. Jie Du
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Rutao Liu.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Yang, B., Liu, R., Hao, X. et al. The Interactions of Glutathione-Capped CdTe Quantum Dots with Trypsin. Biol Trace Elem Res 146, 396–401 (2012). https://doi.org/10.1007/s12011-011-9262-z

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s12011-011-9262-z

Keywords

Search

Navigation