Recent advances in self-assembled peptides: Implications for targeted drug delivery and vaccine engineering

Abstract

Self-assembled peptides have shown outstanding characteristics for vaccine delivery and drug targeting. Peptide molecules can be rationally designed to self-assemble into specific nanoarchitectures in response to changes in their assembly environment including: pH, temperature, ionic strength, and interactions between host (drug) and guest molecules. The resulting supramolecular nanostructures include nanovesicles, nanofibers, nanotubes, nanoribbons, and hydrogels and have a diverse range of mechanical and physicochemical properties. These molecules can be designed for cell-specific targeting by including adhesion ligands, receptor recognition ligands, or peptide-based antigens in their design, often in a multivalent display. Depending on their design, self-assembled peptide nanostructures have advantages in biocompatibility, stability against enzymatic degradation, encapsulation of hydrophobic drugs, sustained drug release, shear-thinning viscoelastic properties, and/or adjuvanting properties. These molecules can also act as intracellular transporters and respond to changes in the physiological environment. Furthermore, this class of materials has shown sequence- and structure-dependent impacts on the immune system that can be tailored to non-immunogenic for drug targeting, and immunogenic for vaccine delivery. This review explores self-assembled peptide nanostructures (beta sheets, alpha helices, peptide amphiphiles, amino acid pairing, elastin like polypeptides, cyclic peptides, short peptides, Fmoc peptides, and peptide hydrogels) and their application in vaccine delivery and drug targeting.

Recent advances in shear‐thinning and self‐healing hydrogels for biomedical applications

“…The stability and unfolding of coiled‐coil motifs are dependent on temperature, pH, and ionic strength, which is often used in the design of stimuli‐responsive controlled release systems . The unique association–dissociation of coiled‐coils make them an ideal candidate for physical crosslinkers to form protein‐based supramolecular fibrils . The incorporation of leucine‐zipper (LZ) domains to the protein backbone created a functional chimeric protein with self‐assembling properties, allowing this self‐assembly strategy to be used in a variety of biomedical applications.…”

Low-Molecular-Weight Gels: The State of the Art

“…15 Ready gel formation by a simple trigger can also be used to allow easy and efficient gel loading. [16][17][18] Unsurprisingly, therefore, there is significant interest in these materials ( Figure 1). This is a fascinating area and in many ways holds attention because of the difficulties in probing and understanding the gels.…”

Biopolymers and Their Composites for Drug Delivery: A Brief Review

“…Numerous delivery techniques, taking advantage of the biochemical interactions (e.g., adhesion ligands, receptor recognition ligands, or peptide‐based antigens), actively target specific cells . Accordingly, reducing the side effects by ducking healthy host tissues, and thus therapeutic index can be increased by accumulating the drug at the diseased site.…”