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Probing the interaction between recombinant human myelin basic protein and caseins using surface plasmon resonance

Medhat A Al-Ghobashy1, Aurelie Cucheval, Martin A K Williams

  • 1Institute of Fundamental Sciences, Massey University, Palmerston North, New Zealand.

Journal of Molecular Recognition : JMR
|October 27, 2009
PubMed
Summary

Transgenic cows produced recombinant human myelin basic protein (rhMBP) that binds to casein micelles via calcium bridges. This interaction, driven by rhMBP phosphorylation, did not alter milk micelle size or charge due to low expression levels.

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Area of Science:

  • Biotechnology
  • Biochemistry
  • Molecular Biology

Background:

  • Human myelin basic protein (hMBP) is intrinsically unstructured.
  • Transgenic cows (TGmilk) were developed to express hMBP in milk, where it associates with casein micelles.

Purpose of the Study:

  • To investigate the interaction between recombinant hMBP (rhMBP) and milk caseins.
  • To determine the mechanism and extent of rhMBP's association with casein micelles.

Main Methods:

  • Surface Plasmon Resonance (SPR) to study protein-protein interactions.
  • Diffusing Wave Spectroscopy (DWS) to analyze casein micelle size and surface charge.

Main Results:

  • A calcium-mediated interaction was observed between rhMBP and caseins, with binding strength correlating to casein phosphorylation levels.
  • The recombinant protein showed selective interaction with caseins, suggesting higher phosphorylation than native hMBP.
  • No significant differences in casein micelle size or surface charge were detected between transgenic and control milk, attributed to low rhMBP expression.

Conclusions:

  • Co-expression and rhMBP's calcium-binding ability facilitate its association with casein micelles.
  • The phosphorylation state of rhMBP is crucial for its interaction with caseins.
  • Low expression levels of rhMBP in transgenic milk prevent alterations in casein micelle structure.