Conformation and self-assembly changes of isomeric peptide amphiphiles influenced by switching tyrosine in the sequences-Reference-Cited by-同舟云学术

Conformation and self-assembly changes of isomeric peptide amphiphiles influenced by switching tyrosine in the sequences

Published:2017 Issue:26 Volume:5 Page:5189-5195
ISSN:2050-750X
Container-title:Journal of Materials Chemistry B
language:en
Short-container-title:J. Mater. Chem. B

Author:

Zhao Fangyi¹²³⁴⁵,Guo Hui¹²³⁴⁵,Zhang Zhidong¹²³⁴⁵,Ye John⁶⁷⁸,Liu Longlong⁶⁷⁸,Zhao Chun-Xia⁹¹⁰¹¹¹²,Shao Zhengzhong¹²³⁴⁵^ORCID

Affiliation:

1. State Key Laboratory of Molecular Engineering of Polymers

2. Laboratory of Advanced Materials and Department of Macromolecular Science

3. Fudan University

4. Shanghai 200433

5. China

6. Peptide Scientific Inc.

7. Fairfiled NJ 07004

8. USA

9. Australian Institute for Bioengineering and Nanotechnology

10. The University of Queensland

11. St. Lucia

12. Australia

Abstract

By simply switching the location of Tyr in isomeric peptide amphiphiles of C₁₂-(GA)₃GY, the varied conformations between the β-sheet and disordered one of these peptide amphiphiles and the alternating morphologies between nanofibers and nanospheres of their assemblies are revealed.

Funder

National Natural Science Foundation of China

Australian Research Council

Publisher

Royal Society of Chemistry (RSC)

Subject

General Materials Science,Biomedical Engineering,General Chemistry,General Medicine

Link

http://pubs.rsc.org/en/content/articlepdf/2017/TB/C7TB00736A

Reference36 articles.

1. Self-assembled peptide nanostructures: the design of molecular building blocks and their technological utilization

2. Integrating top-down and self-assembly in the fabrication of peptide and protein-based biomedical materials