Interfacial properties of lysozyme nanofibrils

Lysozyme is a one of the globular proteins that acts as an antimicrobial enzyme. Its antibacterial properties derived from the ability to hydrolyze the cell wall in gram-positive bacterial. In birds, hen egg white lysozyme is an abundant protein that functions both as an antibiotic as well as a nutrient for early embryogenesis.

However, the lysozyme protein has also a dark side…

Alongside with the important contribution of this protein to the immune system, human lysozyme has been identified as an amyloidogenic type of protein with a high tendency to form fibrillar constructs. The lysozyme fibrils, here refer as aggregates, have tendency to accumulate in human organs, including spleen, liver, and kidney. Such accumulation directly linked to organs dysfunction phenomenon, also known as systemic amyloidosis.¹

For at least two decades the lysozyme’s aggregation mechanism has been studied in details. The investigation of misfolding² and aggregation behavior of lysozyme proteins showed that fibril formation take place when native state of lysozyme destabilized creating a difference in the energy barrier between the native state and partially unfolded intermediates.¹

My research focuses on investigation the link between the interfacial properties, including kinetics and dynamics of lysozyme protein fibrillation³, which could potentially lead to a better understanding of the general aggregation mechanism in self-assembling biopolymers.⁴ In particular I am interested in looking at the adsorptive properties⁵ of lysozyme-based material. Herein, I will present the effect of controlled self-assembly and the derived adsorptive properties of lysozyme protein fibrils.

References:

[1] Kumita, J., FASEB 26, 192 (2012).

[2] Dobson, C., Nature 426, 884 (2003).

[3] Shimanovich, U., ACSNano 9, 43 (2015).

[3] Mason, T. O, Adv. Mater 1706462 (2018).

[3] Jordens, S., ACSNano 8, 11071 (2014).