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Molecules 2019, 24(1), 202; https://doi.org/10.3390/molecules24010202

Self-Assembly of Short Elastin-like Amphiphilic Peptides: Effects of Temperature, Molecular Hydrophobicity and Charge Distribution

1
State Key Laboratory of Heavy Oil Processing and Centre for Bioengineering and Biotechnology, China University of Petroleum (East China), 66 Changjiang West Road, Qingdao Economic Development Zone, Qingdao 266580, China
2
Personnel Department and School of Blue Economy Engineering, Qingdao Vocational and Technical College, Qingdao Economic and Technological Development Zone, Qingdao 266555, China
3
Shandong Key Laboratory of Biochemical Analysis, College of Chemistry and Molecular Engineering, Qingdao University of Science and Technology, Qingdao 266042, China
*
Author to whom correspondence should be addressed.
Academic Editor: He Dong
Received: 21 December 2018 / Revised: 31 December 2018 / Accepted: 7 January 2019 / Published: 8 January 2019
(This article belongs to the Special Issue Recent Advances in Self-Assembled Peptides)
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Abstract

A novel type of self-assembling peptides has been developed by introducing the basic elastomeric β-turn units of elastin protein into the amphiphilic peptide molecules. The self-assembly behaviors of such peptides are affected by the overall molecular hydrophobicity, charge distribution and temperature. The molecules with higher hydrophobicity exhibit better self-assembling capability to form long fibrillar nanostructures. For some peptides, the temperature increase can not only promote the self-assembly process but also change the self-assembly routes. The self-assembly of the peptides with two charges centralized on one terminal show higher dependence on temperature than the peptides with two charges distributed separately on the two terminals. The study probes into the self-assembly behaviors of short elastin-like peptides and is of great help for developing novel self-assembling peptides with thermo sensitivity. View Full-Text
Keywords: amphiphilic peptides; elastin-like peptides; elastomeric β-turn units; temperature-sensitivity; self-assembly amphiphilic peptides; elastin-like peptides; elastomeric β-turn units; temperature-sensitivity; self-assembly
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Cao, M.; Shen, Y.; Wang, Y.; Wang, X.; Li, D. Self-Assembly of Short Elastin-like Amphiphilic Peptides: Effects of Temperature, Molecular Hydrophobicity and Charge Distribution. Molecules 2019, 24, 202.

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