In silico physicochemical characterization and comparison of two intrinsically disordered phosphoproteins: β-casein and acidic PRP-1

Research output: Contribution to journalArticle


A coarse-grained model has been implemented using the Metropolis-Hastings Monte Carlo method to simulate β-casein and acidic proline-rich protein 1 (PRP-1). The aim of the study is to directly compare the properties and behavior of β-casein and PRP-1, in both bulk solution and in the presence of a negatively charged surface, in order to evaluate the possibility of using β-casein as a replacement for PRP-1 in, e.g. saliva substitutes and, possibly, dental products. The results are obtained by studying the effect of varying pH, monovalent salt concentration and with/without charge saturation of the phosphorylated serines. The electrostatic properties in bulk are found to be very similar for the two proteins, especially at physiological pH and with simulated calcium saturation. When studying surface adsorption it is observed that both proteins attach to the surface in similar ways, relatively to their size. Surface adsorption seems to be stronger for PRP-1, but β-casein is shown to adsorb closer to the surface. The adsorption of both proteins onto the negatively charged surface is strikingly similar under physiological pH and higher, near physiological, salt concentrations. The effect of calcium saturation on surface adsorption is almost negligible for both proteins at high salt concentration.


Research areas and keywords

Subject classification (UKÄ) – MANDATORY

  • Physical Chemistry


  • Acidic PRP-1, Intrinsically disordered protein, Monte Carlo simulation, Phosphoprotein, Surface adsorption, β-casein
Original languageEnglish
Pages (from-to)360-371
Number of pages12
JournalFood Hydrocolloids
Publication statusPublished - 2016 May 1
Publication categoryResearch

Related research output

Joao Henriques, 2016 Nov, Lund: Lund University, Faculty of Science, Department of Chemistry, Theoretical Chemistry. 90 p.

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