Skip to main content
SpringerLink
Log in

A New Artificial Chaperone for Protein Refolding: Sequential Use of Detergent and Alginate

  • Published:
The Protein Journal Aims and scope Submit manuscript

Abstract

A novel artificial chaperone system using a combination of detergents and alginate was developed to refold three enzymes with totally different structures. Upon dilution of denatured protein in the presence of the capturing agent, complexes of the detergent and non-native protein molecules are formed and thereby the formation of protein aggregates is prevented. The so-called captured protein is unable to refold from the detergent-protein complex states unless a stripping agent is used to gradually remove the detergent molecules. In that respect, we used alginate, a linear copolymer of d-mannuronic acid and l-guluronic acid, to initiate and complete the refolding process. The results indicated that the extent of refolding assistance for the proteins was different due to detergent structure and also the length of hydrophobic portion of each detergent. These observed differences were attributed to the strong electrostatic and hydrophobic interactions among the capturing and stripping agents used in this investigation. Based on this newly developed method, it is expected that the protein refolding operation can be achieved easily, cheaply and efficiently.

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

Fig. 1
Fig. 2
Fig. 3
Fig. 4
Fig. 5

Similar content being viewed by others

Abbreviations

α-CD:

α-Cyclodextrin

ALP:

Alkaline phosphatase

BSA:

Bovine serum albumin

CA:

Carbonic anhydrase

CTAHS:

Cetyltrimethylammonium hydrogen sulfate

CTAB:

Cetyltrimethylammonium bromide

DTAB:

Dodecyl trimethylammonium bromide

GuHCl:

Guanidine hydrochloride

pNPAc:

p-Nitrophenyl acetate

pNPP:

p-Nitrophenyl phosphate

SHS:

Sodiumhexadecyl sulfate

STS:

Sodiumtetradecyl sulfate

SDS:

Sodiumdodecyl sulfate

TTAB:

Tetradecyl trimethylammonium bromide

References

  1. Goldberg ME, Ruldoph R, Jaenicke R (1991) Biochemistry 30:2790–2797

    Article  CAS  Google Scholar 

  2. Cleland JL, Builder SE, Swartz JR, Winkler M, Chang JY, Wang DIC (1992) Biotechnology 10:1013–1019

    Article  CAS  Google Scholar 

  3. Fisher B, Sumner I, Goodenough P (1993) Arch Biochem Biophys 306:183–187

    Article  Google Scholar 

  4. Ou WB, Park YD, Zhou HM (2002) Cell Biol 34:136–147

    CAS  Google Scholar 

  5. Zancan P, Sola-Penna M (2005) Arch Biochem Biophys 444:52–60

    Article  CAS  Google Scholar 

  6. Tayyab S, Ahmad B, Kumar Y, Khan MM (2002) J Biol Macromol 30:17–22

    Article  CAS  Google Scholar 

  7. Meng FG, Park YD, Zhou HM (2001) Int J Biochem Cell Biol 33:701–709

    Article  CAS  Google Scholar 

  8. Kumar Y, Muzammil S, Tayyeb S (2005) Biochemistry (Tokyo) 138:335–341

    CAS  Google Scholar 

  9. Tandon S, Horowitz PM (1987) J Biol Chem 262:4486–4491

    CAS  Google Scholar 

  10. Muzammil S, Kumar Y, Tayyab S (2000) Biochem Biophys Acta 1476:139–148

    CAS  Google Scholar 

  11. Zhang YX, Zhu YH, Xi W, Liu YL, Zhou HM (2002) Int J Biochem Cell Biol 34:1241–1247

    Article  CAS  Google Scholar 

  12. Tian XJ, Song XH, Yan SL, Zhang YX, Zhou HM (2003) J Protein Chem 22:417–422

    Article  CAS  Google Scholar 

  13. Karuppiah N, Sharma A (1995) Biochem Biophys Res Commun 211:60–66

    Article  CAS  Google Scholar 

  14. Khodarahmi R, Yazdanparast R (2004) Biochem Biophys Acta 1647:175–181

    Google Scholar 

  15. Rozema D, Gellman SH (1995) J Am Chem Soc 117:2373–2374

    Article  CAS  Google Scholar 

  16. Couthon F, Clottes E, Vial C (1996) Biochem Biophys Res Commun 227:854–860

    Article  CAS  Google Scholar 

  17. Rozema R, Gellman SH (1996) J Biol Chem 271:3478–3487

    Article  CAS  Google Scholar 

  18. Hanson PE, Gellman SH (1998) Fold Des 3:457–468

    Article  CAS  Google Scholar 

  19. Wang J, Lu D, Lin Y, Liu Zh (2005) Biochem Eng J 24:269–277

    Article  CAS  Google Scholar 

  20. Sivakama Sundari C, Raman B, Balasubramanian D (1999) FEBS Lett 443:215–219

    Article  CAS  Google Scholar 

  21. Machida S, Ogawa S, Xiaohua SH, Takaha T, Fujii K, Hayashi K (2000) FEBS Lett 486:131–135

    Article  CAS  Google Scholar 

  22. Wan LSC, Heng PWS (1992) J Microencapsulation 9:309–316

    Article  CAS  Google Scholar 

  23. Sugawara S, Imai T, Otagiri M (1994) Pharmaceut Res 11:272–277

    Article  CAS  Google Scholar 

  24. Ren B, Gao Y, Lu L, Liu X, Tong Z (2006) Carbohydr Polym 66:263–273

    Article  Google Scholar 

  25. Neumann MG, Schmitt CC, Iamazaki ET (2003) Carbohydr Res 338:1109–1113

    Article  CAS  Google Scholar 

  26. Bu H, Kjoniksen AL, Knudsen KD, Nystrom B (2005) Longmuir 21:10923–10930

    Article  CAS  Google Scholar 

  27. Khodagholi F, Yazdanparast R (2005) Protein J 24:303–313

    Article  CAS  Google Scholar 

  28. Khodarahmi R, Yazdanparast R (2005) Int J Biol Macromol 36:191–197

    Article  CAS  Google Scholar 

  29. Yazdanparast R, Khodagholi F (2006) Arch Biochem Biophys 446:11–19

    Article  CAS  Google Scholar 

  30. Garen A, Levinthal C (1960) Biochem Biophys Acta 38:470–483

    Article  CAS  Google Scholar 

  31. Pocker Y, Stone J (1967) Biochemistry 6:668–675

    Article  CAS  Google Scholar 

  32. Bernfeld P (1951) Inter science publ 379

  33. Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) J Biol Chem 193:265–275

    CAS  Google Scholar 

  34. Debye P, Huckel E (1923) Phys Z 24:185–206

    CAS  Google Scholar 

  35. Glazer AN, Smith EL (1961) J Biol Chem 236:2942–2946

    CAS  Google Scholar 

  36. Xu GJ, Tsou CL (1963) Acta Biochem Biophys Sin 3:450–458

    Google Scholar 

  37. Guex N, Peitsch MC (1997) Electrophoresis 18:2714–2723

    Article  CAS  Google Scholar 

  38. Mondal K, Bohidar HB, Roy RP, Gupta MN (2006) Biochem Biophys Acta 5:877–886

    Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Institute of Biochemistry and Biophysics, The University of Tehran, P.O. Box 13145-1384, Tehran, Iran

    Fariba Khodagholi, Bahareh Eftekharzadeh & Razieh Yazdanparast

Authors
  1. Fariba Khodagholi
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Bahareh Eftekharzadeh
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. Razieh Yazdanparast
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Razieh Yazdanparast.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Khodagholi, F., Eftekharzadeh, B. & Yazdanparast, R. A New Artificial Chaperone for Protein Refolding: Sequential Use of Detergent and Alginate. Protein J 27, 123–129 (2008). https://doi.org/10.1007/s10930-007-9115-y

Download citation

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s10930-007-9115-y

Keywords

Search

Navigation