Bolaamphiphile,
which is a class of amphiphilic molecules, has
a unique structure of two hydrophilic head groups at the ends of the
hydrophobic center. Peptidic bolaamphiphiles that employ peptides
or amino acids as their hydrophilic groups exhibit unique biochemical
activities when they self-organize into supramolecular structures,
which are not observed in a single molecule. The self-assembled peptidic
bolaamphiphiles hold considerable promise for imitating proteins with
biochemical activities, such as specific affinity toward heterogeneous
substances, a catalytic activity similar to a metalloenzyme, physicochemical
activity from harmonized amino acid segments, and the capability to
encapsulate genes like a viral vector. These diverse activities give
rise to large research interest in biomaterials engineering, along
with the synthesis and characterization of the assembled structures.
This review aims to address the recent progress in the applications
of peptidic bolaamphiphile assemblies whose densely packed peptide
motifs on their surface and their stacked hydrophobic centers exhibit
unique protein-like activity and designer functionality, respectively.
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