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Self-Assembly Mechanism of a Peptide-Based Drug Delivery Vehicle.


ABSTRACT: We report the mechanism of the concentration-dependent self-assembly of a tetrapeptide. Peptide Boc-Trp-Leu-Trp-Leu-OMe self-assembles to form discrete nanospheres at a low concentration. Tryptophan side chains point outwards of the nanospheres while leucine side chains point towards the core of the nanospheres. The nanospheres fuse together to become microspheres with the increase in the peptide concentration. At higher concentrations of the peptide, the microspheres start clustering. This is stabilized by the aromatic interactions between the side chains of the tryptophan residues that cover the outer surface of the peptide microspheres. In addition to behaving like the conventional hollow sphere-based drug delivery vehicles which entraps the drug and performs stimuli-responsive release, this prototype can interact, stabilize, and intercalate hydrophobic dye carboxyfluorescein and anti-cancer drug curcumin even on the surface through aromatic interactions. The dye/drug can be released in acidic pH and in the presence of physiologically relevant ions such as potassium.

SUBMITTER: Pandit G 

PROVIDER: S-EPMC6045401 | biostudies-literature | 2018 Mar

REPOSITORIES: biostudies-literature

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Self-Assembly Mechanism of a Peptide-Based Drug Delivery Vehicle.

Pandit Gopal G   Roy Karabi K   Agarwal Umang U   Chatterjee Sunanda S  

ACS omega 20180315 3


We report the mechanism of the concentration-dependent self-assembly of a tetrapeptide. Peptide Boc-Trp-Leu-Trp-Leu-OMe self-assembles to form discrete nanospheres at a low concentration. Tryptophan side chains point outwards of the nanospheres while leucine side chains point towards the core of the nanospheres. The nanospheres fuse together to become microspheres with the increase in the peptide concentration. At higher concentrations of the peptide, the microspheres start clustering. This is s  ...[more]

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