Rational design of amphiphilic fluorinated peptides: evaluation of self-assembly properties and hydrogel formation-Reference-Cited by-同舟云学术

Rational design of amphiphilic fluorinated peptides: evaluation of self-assembly properties and hydrogel formation

Published:2022 Issue:28 Volume:14 Page:10176-10189
ISSN:2040-3364
Container-title:Nanoscale
language:en
Short-container-title:Nanoscale

Author:

Chowdhary Suvrat¹^ORCID,Schmidt Robert Franz²,Sahoo Anil Kumar³⁴^ORCID,tom Dieck Tiemo¹,Hohmann Thomas¹^ORCID,Schade Boris⁵^ORCID,Brademann-Jock Kerstin⁶,Thünemann Andreas F.⁶^ORCID,Netz Roland R.³^ORCID,Gradzielski Michael²^ORCID,Koksch Beate¹^ORCID

Affiliation:

1. Institute of Chemistry and Biochemistry, Freie Universität Berlin, Arnimallee 20, 14195 Berlin, Germany

2. Institute of Chemistry, Technische Universität Berlin, Straße des 17. Juni 124, 10623 Berlin, Germany

3. Department of Physics, Freie Universität Berlin, Arnimallee 14, 14195 Berlin, Germany

4. Max Planck Institute of Colloids and Interfaces, Am Mühlenberg 1, 14476 Potsdam, Germany

5. Institute of Chemistry and Biochemistry and Core Facility BioSupraMol, Freie Universität Berlin, Fabeckstraße 36a, 14195 Berlin, Germany

6. Federal Institute for Materials Research and Testing (BAM), Unter den Eichen 87, 12205 Berlin, Germany

Abstract

The tremendous impact of fluorine-specific interactions on peptide folding and self-assembly was systematically studied. Therefore, the fluorinated aliphatic amino acids MfeGly, DfeGly and TfeGly were incorporated into an amphipathic peptide motif.

Funder

Deutsche Forschungsgemeinschaft

Publisher

Royal Society of Chemistry (RSC)

Subject

General Materials Science

Link

http://pubs.rsc.org/en/content/articlepdf/2022/NR/D2NR01648F

Reference74 articles.

1. Biomimetic peptide self-assembly for functional materials

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3. Responsive Hydrogels from the Intramolecular Folding and Self-Assembly of a Designed Peptide