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Multifunctional Self-Assembling Peptide-Based Nanostructures for Targeted Intracellular Delivery: Design, Physicochemical Characterization, and Biological Assessment.

Peptide amphiphiles (PAs), consisting of a hydrophobic alkyl chain covalently bound to a hydrophilic peptide sequence, possess a versatile molecular design due to their combined self-assembling features of amphiphile surfactants and biological functionalities of peptides. Through rational design, PAs can self-assemble into a variety of nanostructures with controlled shape, size, and biological functionality to deliver therapeutic and imaging agents to target cells. Here, we describe principles to design multifunctional PAs for self-assembly into micellar nanostructures and targeted intracellular delivery. The PA micelles are designed to display a tumour targeting sequence on their surfaces and direct their interactions with specific cells. This targeting sequence includes an enzymatic sensitive sequence that can be cleaved upon exposure to matrix metalloproteinase 2 (MMP-2), an enzyme overexpressed in tumor environment, allowing the presentation of a cell-penetrating domain. The presentation of this domain will then facilitate the delivery of therapeutics for cancer treatment inside targeted cells. Methods to characterize the key physicochemical properties of PAs and their assemblies, including secondary structure, critical micelle concentration, shape and size, are described in detail. The enzyme responsiveness of PA assemblies is described with respect to their degradation by MMP-2. Protocols to evaluate the cytotoxicity and cellular uptake of the micellar carriers are also included.

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