Skip to main content
Log in

Induction of changes in the secondary structure of globular proteins by a hydrophobic surface

  • Published:
European Biophysics Journal Aims and scope Submit manuscript

Abstract

Circular dichroism, ellipsometry and radiolabeling techniques were employed to study the induction of changes in the secondary structure of BSA, myoglobin and cytochrome C by a hydrophobic surface. The results showed that adsorbed protein molecules lose their ordered native structure in the initial stage of adsorption and the structure appears to be a random or disordered conformation. Protein molecules adsorbed in later stages adopt a more ordered secondary structure (α helix and β structure). The changes of secondary structure of globular proteins induced by a hydrophobic surface can be explained by the steric interaction between adsorbed proteins as well as by hydrophobic interactions during the adsorption process. In addition, there is obviously an intermediate stage in which the protein molecules are mainly in the β structure, indicating that for certain proteins, the β structure may be a more stable secondary structure than α helix on the hydrophobic surface.

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

Access this article

Subscribe and save

Springer+ Basic
EUR 32.99 /Month
  • Get 10 units per month
  • Download Article/Chapter or Ebook
  • 1 Unit = 1 Article or 1 Chapter
  • Cancel anytime
Subscribe now

Buy Now

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

Instant access to the full article PDF.

Similar content being viewed by others

References

  • Horsley D, Herron J, Hlady V, Andrade JD (1991) Fluorescence quenching of adsorbed hen and human lysozymes. Langmuir 7(2): 218–222

    Google Scholar 

  • Kop JMM, Cuypers PA, Lindhout T, Hemker HC, Hermer WT (1984) The adsorption of prothrombin to phospholipid monolayer quantitated by ellipsometry. J Biol Chem 259(22): 13993–13998

    Google Scholar 

  • Lee SH, Ruckenstein E (1988) Adsorption of proteins onto polymeric surface of different hydrophilicities — a case study with bovine serum albumin. J Colloid Interface Sci 125(2): 365–379

    Google Scholar 

  • Lenk TJ, Horbett TA, Ratner BD (1991) Infrared spectroscopic studies of time-dependent changes in fibrinogen adsorbed to polyurethanes. Langmuir 7(8): 1755–1759

    Google Scholar 

  • Lu DR, Park K (1991) Effect of surface hydrophobicity on the conformational changes of adsoraed fibrinogen. J Colloid Interface Sci 144: 271–281

    Google Scholar 

  • Reddy GL, Nagaraj R (1989) Circular dichroism studies on synthetic signal peptide indicate β-conformation as a common structural feature in highly hydrophobic environment. J Biol Chem 264: 16591–16597

    Google Scholar 

  • Schmidt CF, Zimmermann RM, Gaub HE (1990) Multilayer adsorption of lysozyme on a hydrophobic structure. Biophys J 57: 577–588

    Google Scholar 

  • Soderquist ME, Walton AG (1980) Structure changes in proteins adsorbed on polymer surface. J Colloid Interface Sci 75: 386–398

    Google Scholar 

  • Stevens L, Townend R, Timasheff SN, Fasman GD, Potter J (1968) The circular dichroism of polypeptide films. Biochemistry 7(10): 3717–3720

    Google Scholar 

  • Wu H, Sui SF (1992) Adsorption of bovine serum albumin at the solid/liquid interface quantitated by in situ ellipsometry. Acta Biophys Sinica 8(2): 245–251

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Additional information

Correspondence to: S.-F. Sui

Rights and permissions

Reprints and permissions

About this article

Cite this article

Wu, H., Fan, Y., Sheng, J. et al. Induction of changes in the secondary structure of globular proteins by a hydrophobic surface. Eur Biophys J 22, 201–205 (1993). https://doi.org/10.1007/BF00185781

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF00185781

Key words

Navigation