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

Rie Wakabayashi; Ayumi Suehiro; Masahiro Goto; Noriho Kamiya

doi:10.1039/C8CC08163H

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

Rie Wakabayashi, Ayumi Suehiro, Masahiro Goto, Noriho Kamiya

Research output: Contribution to journal › Article

5 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 language	English
Pages (from-to)	640-643
Number of pages	4
Journal	Chemical Communications
Volume	55
Issue number	5
DOIs	https://doi.org/10.1039/C8CC08163H
Publication status	Published - Jan 1 2019

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

Access to Document

10.1039/C8CC08163H

Fingerprint Dive into the research topics of 'Designer aromatic peptide amphiphiles for self-assembly and enzymatic display of proteins with morphology control'. Together they form a unique fingerprint.

Cite this

Wakabayashi, R., Suehiro, A., Goto, M., & Kamiya, N. (2019). Designer aromatic peptide amphiphiles for self-assembly and enzymatic display of proteins with morphology control. Chemical Communications, 55(5), 640-643. https://doi.org/10.1039/C8CC08163H

@article{e2da4ffe247247cd8e3ff43a3f87c28e,

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",

month = jan,

day = "1",

doi = "10.1039/C8CC08163H",

language = "English",

volume = "55",

pages = "640--643",

journal = "Chemical Communications",

issn = "1359-7345",

publisher = "Royal Society of Chemistry",

number = "5",

}

TY - JOUR

T1 - Designer aromatic peptide amphiphiles for self-assembly and enzymatic display of proteins with morphology control

AU - Wakabayashi, Rie

AU - Suehiro, Ayumi

AU - Goto, Masahiro

AU - Kamiya, Noriho

PY - 2019/1/1

Y1 - 2019/1/1

N2 - 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.

AB - 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.

UR - http://www.scopus.com/inward/record.url?scp=85059760006&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85059760006&partnerID=8YFLogxK

U2 - 10.1039/C8CC08163H

DO - 10.1039/C8CC08163H

M3 - Article

C2 - 30628590

AN - SCOPUS:85059760006

VL - 55

SP - 640

EP - 643

JO - Chemical Communications

JF - Chemical Communications

SN - 1359-7345

IS - 5

ER -