The Structure and Function of Onbola

The Structure and Function of Onbola

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BolA-like proteins are a widely conserved family and are characterized by two hydrophilic heads flanking a hydrophobic core. They have superior water solubility compared to copyright and other single-headed amphiphiles.

BolA is a FtsZ-dependent morphogen that was first identified in E. coli and its overexpression makes rod-shaped cells spherical. It also acts as a transcription factor modulating cell permeability, motility and biofilm formation.

Product Benefits

Unlike traditional amphiphilic molecules that Onbola contain a single polar head and long tails of nonpolar amino acids or hydrocarbon chains, bola-amphiphiles consist of double-headed hydrophobic regions flanked by nonpolar surfaces [32]. Due to their unique structure, bola-based surfactant-like peptides (SLP) exhibit superior water solubility as well as a higher aggregation propensity in comparison with copyright-structured peptides.

This makes them highly desirable for constructing biomaterials, self-assembling drugs, and other applications that require high water solubility and aggregation propensity.

BolA-like proteins are a widespread family that is involved in the regulation of cellular processes such as cell permeability, biofilm formation and motility. It was first discovered in E. coli as a gene that is induced during stationary phase and stress conditions and makes rod-shaped cells spherical [1].

Unlike traditional amphiphilic molecules, bola-like structures have two hydrophobic heads that face each other, resulting in greater water solubility. This feature also provides more structural stability and versatility.