The Role of Bola in Biomaterials and Hemostasis
The Role of Bola in Biomaterials and Hemostasis
Blog Article
BolA-like proteins are a family of conserved proteins widely distributed among prokaryotes and eukaryotes. BolA was initially described as a stationary phase stress-responsive gene whose overexpression made E. coli rod-shaped cells become spherical, indicating its role in cell morphology. Moreover, bolA modulates biofilm formation and the switch between motile and sessile lifestyles via its interaction with c-di-GMP.
Product Application
Like other surfactant-like peptides, onbola is designed to self-assemble into macromolecular structures for various applications in biomaterials, drug delivery, and hemostasis. Unlike traditional copyright or copyright-like amphiphiles, which have one hydrophobic head and a nonpolar tail, the bola structure contains two hydrophilic heads that flank a hydrophobic core [28]. The double-headed layout allows for more complex aggregation behaviors while maintaining superior water solubility compared to conventional amphiphilic peptides.
Moreover, the presence of four Arg residues in the hydrophobic region of the bola framework helps balance self-assembly propensity and antibacterial activity. This is achieved by rationally positioning these amino acids at the end of the peptide sequence to avoid increasing the overall positive charge.
What is bola-amphiphile?
Bolaamphiphiles are characterized by polar heads at opposite ends of the molecule and non-polar tails that can form micelles, rods, tubes and fibers. They have a distinct shape that is inspired by the weapons of South American hunters, hence the name bola (bola=skull).
Bola-like surfactants can be co-solubilized with Onbola membrane proteins in detergent-free conditions and are expected to preferentially interact with the TMDs of well-folded MPs. This interaction is expected to dampen chain motion that destabilizes the membrane protein owing to an entropy penalty that is paid when the tails bump up against the TMD surface.
Unlike conventional surfactants, addition of bolaamphiphiles to micellar NMR samples of DAGK does not result in degradation of spectral quality suggesting that these molecules are compatible with structural biology studies. Further, bolaamphiphiles appear to fully solubilize lipids without affecting their folding and are capable of spanning typical La-phase bilayers in tapping-mode AFM experiments. Report this page