Abstract
It is crucial for hydrophobic drugs to be dissolved and stabilized by carriers in aqueous systems and then to be delivered into target cells. An amphiphilic self‐assembling peptide EAK16‐I (Ac‐AEAKAEAKAEAKAEAK‐NH2) is reported here to be able to stabilize a model hydrophobic compound, pyrene, in aqueous solution, resulting in the formation of colloidal suspensions. Egg phosphatidylcholine (EPC) vesicles are used as plasma membranes mimic. Fluorescence data shows that the pyrene is presented in the crystalline form when stabilized by EAK16‐I and molecularly migrates from its peptide encapsulations into the membrane bilayers of EPC vesicles when the suspension is mixed with EPC vesicles. Furthermore, the release rate can be controlled by changing peptide‐to‐pyrene ratio, and the higher ratios lead to the slower release rates due to a thicker encapsulation on the pyrene microcrystals. This demonstrates that EAK16‐I, as a promising nanobiomaterial, has the potential to be a hydrophobic compounds carrier.
Highlights
Low water solubility limits the clinical practice of many potent hydrophobic drugs [1]
The purpose of this study is to examine whether EAK16I can stabilize microcrystals of pyrene, a hydrophobic compound, in aqueous solution and deliver them into the membrane of a cell mimic made of the egg phosphatidylcholine (EPC) vesicles
In the presence of the peptide EAK16-I, a milk-white colloidal suspension was obtained after stirring the EAKI-PY aqueous mixture for 3 hours, while the control sample without peptide still remained transparent with pyrene crystals floating on the top or precipitating at the bottom
Summary
Low water solubility limits the clinical practice of many potent hydrophobic drugs [1]. By (re-)designing the amino acid sequences, self-assembling peptides (8–16 residues, 2.5–5 nm in length) [3], with good biocompatibility, have already been used in versatile biomedical applications, such as cell cultures, tissue engineering, and surface engineering [4,5,6], while only a few studies had been reported to investigate the applicability of self-assembling peptides as drug carriers [7,8,9]. At neutral pH, Glu and Lys are negatively and positively charged, respectively They are believed to form complementary ion pairs when EAK16-I self-assembles into its β-sheet microstructure which exhibits a hydrophobic and a hydrophilic surfaces. It is expected that the hydrophobic region of EAK16-I can interact with hydrophobic compounds while the charged residues stabilize the complex in aqueous solution
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