Chalmers Conferences, 9th European Conference on Mathematical and Theoretical Biology

Mechanism of The Nanodiamond – Protein Collective Aggregation
Peter I Belobrov

Last modified: 2014-03-28


Nanodiamonds selectively absorb recombinant apoobelin and luciferase from Escherichia coli bacterial cells [1]. The method allows to extract purified proteins from a mixture by a simple rapid procedure. However, the underlying mechanism of protein – nanodiamond co-aggregation is not still completely understood. We propose here a possible explanation for the unusual selectivity of nanodiamond in the process of co-aggreation with apoobelin and luciferase proteins.

Non-native aggregation of proteins is a multi-stage process [2,3], including in a nutshell transition from folding – unfolding equilibrium through the formation of several “reactive” monomers capable of aggregating reversibly to form oligomers. These oligomers in turn could form either amorphous aggregates or complex filaments. Nanodiamond in water solutions is itself capable of rapid aggregation in clusters up to 1-10 μm size and it doesn't undergo folding – unfolding transformations. We suggest that similarity in aggregation kinetic characteristics of folded active monomers and nanodiamond promotes “resonant” collective nanodiamond – protein aggregation. Even though, additional quantitative investigation is required to verify the idea.



[1] Bondar V.S., Pozdnyakova I.O., Puzyr A. P. Applications of nanodiamonds for separation and purification of proteins/ Phys Solid State 46 (4) 758–760  (2004).
[2] Roberts C.J. Non-native protein aggregation kinetics Biotechnol Bioeng 98 (5)  927–938 (2007).
[3] Morris A.M., Watzky M.A., Finke R.G. Protein aggregation kinetics, mechanism, and curve-fitting: a review of the literature Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics 1794 (3) 375–397 (2009).




nanodiamond, protein-diamond collective coaggregation