Abstract
Peptide amphiphiles are one of the most promising materials in the biomedical field, so much effort has been devoted to characterizing the mechanism of their self-assembly and thermosensitive gelation. In this work, vapor pressure osmometry measurements were carried out to parameterize the thermosensitivity of interactions between peptide amphiphiles in an aqueous solution. The osmometry measurement verified that the peptides became more hydrophobic as temperature increased, which was quantitatively described with the Flory–Huggins χ parameter. Thereafter, a coarse-grained molecular model was used to simulate peptide amphiphiles dissolved in an aqueous solution. The temperature sensitive coarse-grained parameter aHW, which is the repulsive force between the hydrophilic head of the peptide amphiphile and water was estimated from the aforementioned experimentally obtained χ. Furthermore, the effects of concentration and temperature on the self-assembly behavior of peptide amphiphiles were quantitatively studied by dissipative particle dynamics. The simulation results revealed that aHW plays an important role in self-assembly characteristics and in the resulting microstructure of the peptide amphiphiles, which coincides with previous experimental and computational findings. The methodology in quantitatively linking the coarse-grained parameter from experiment and theory provides a sensible foundation for bridging future simulation studies with experimental work on macromolecules.
Highlights
Stimuli-responsive polymers are known to change their macroscopic properties based on variations in external conditions such as temperature, pH, light, and magnetic elds
Several studies have revealed that the self-assembly mechanism of Peptide amphiphiles (PA) is more complicated compared to conventional amphiphilic molecules because their assembly behavior is extensively affected by the secondary structure of a-helix and b-sheet transitions.[12,15,16,17,18]
The DFel values obtained for four different NaCl aqueous solutions (0.2–1 wt%) were separated by concentration before being plotted
Summary
Stimuli-responsive polymers are known to change their macroscopic properties based on variations in external conditions such as temperature, pH, light, and magnetic elds. Several studies have revealed that the self-assembly mechanism of PA is more complicated compared to conventional amphiphilic molecules because their assembly behavior is extensively affected by the secondary structure of a-helix and b-sheet transitions.[12,15,16,17,18] Nowak et al.[12] employed rheological and morphological analyses on PA with several peptide sequences and found that gelation was tied to the conformation of the hydrophobic peptide domains They reported that the a-helical segments worked as good gelators, followed by the b-sheet and. The conditions for both methods will be explained, which will be followed by the results and discussion of this work
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