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.
Highlights
Elastin is an insoluble extracellular-matrix protein that imparts elasticity to organs and tissues [1,2,3].Tropoelastin is the soluble precursor of elastin
We can probe into the effects of molecular hydrophobicity and charge distribution on the peptide self-assembly behaviors
The other is that IK-K11 and IK-K16, the peptides with the positive charges separated on the two terminals, gave smaller fibril diameters than their counterparts of IKK11 and IKK16, whose charges are centralized on one terminal
Summary
Elastin is an insoluble extracellular-matrix protein that imparts elasticity to organs and tissues [1,2,3]. Molecules 2019, 24, 202 elastin-derived peptides with limited number (usually 1–5) of the repeating β-turn units have been shown to have similar temperature-sensitive conformational changes as ELPs [20,21,22,23,24,25,26,27,28,29]. It has been found that the ITT temperature of an elastin-like peptide can be tailored through several aspects, such as adjusting the chain length, replacing residues in the repeating unit, varying groups and charges at the termini and so on [22,28,30,31] These findings all serve as foundations for designing novel elastin-based short peptides that have temperature-responsive self-assembling properties [29,32,33,34,35]. It bears great significance for the rational design of temperature-sensitive self-assembling peptides
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