Self-assembling peptidic bolaamphiphiles for biomimetic applications

Hyesung Lee, Hanbee Kim, Sang Yup Lee

Research output: Contribution to journalReview articlepeer-review

1 Citation (Scopus)


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.

Original languageEnglish
Pages (from-to)3545-3572
Number of pages28
JournalACS Biomaterials Science and Engineering
Issue number8
Publication statusPublished - 2021 Aug 9

Bibliographical note

Funding Information:
This study was supported by a grant from the Korean Research Foundation funded by the Korean Government (NRF-2019R1A2C1010629).

Publisher Copyright:
© 2021 American Chemical Society.

All Science Journal Classification (ASJC) codes

  • Biomaterials
  • Biomedical Engineering


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