Designer aromatic peptide amphiphiles for self-assembly and enzymatic display of proteins with morphology control

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2 Citations (Scopus)

Abstract

We herein designed bi-functional aromatic peptide amphiphiles both self-assembling to fibrous nanomaterials and working as a substrate of microbial transglutaminase, leading to peptidyl scaffolds with different morphologies that can be enzymatically post-functionalized with proteins.

Original languageEnglish
Pages (from-to)640-643
Number of pages4
JournalChemical Communications
Volume55
Issue number5
DOIs
Publication statusPublished - Jan 1 2019

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Amphiphiles
Transglutaminases
Nanostructured materials
Scaffolds
Self assembly
Peptides
Display devices
Proteins
Substrates

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Electronic, Optical and Magnetic Materials
  • Ceramics and Composites
  • Chemistry(all)
  • Surfaces, Coatings and Films
  • Metals and Alloys
  • Materials Chemistry

Cite this

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title = "Designer aromatic peptide amphiphiles for self-assembly and enzymatic display of proteins with morphology control",
abstract = "We herein designed bi-functional aromatic peptide amphiphiles both self-assembling to fibrous nanomaterials and working as a substrate of microbial transglutaminase, leading to peptidyl scaffolds with different morphologies that can be enzymatically post-functionalized with proteins.",
author = "Rie Wakabayashi and Ayumi Suehiro and Masahiro Goto and Noriho Kamiya",
year = "2019",
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journal = "Chemical Communications",
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AU - Suehiro, Ayumi

AU - Goto, Masahiro

AU - Kamiya, Noriho

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JO - Chemical Communications

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