Self-assembling peptide-based nanodrug delivery systems

Abstract

The present review outlines the methods designing self-assembling peptide-based NDDs for small molecule drugs, with an emphasis on the different drug delivery strategies and their applications in using peptides and peptide conjugates.

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“…This self-assembly peptide-based drug delivery contains amino acids, which contributes beneficial activity to deliver peptides such as biocompatibility, biodegradability, flexible responsiveness, patientspecific therapy, disease-specific therapy, etc. and most of the drug deliveries are formulated as nanoparticles which control biodistribution, enhance efficacy, reduces toxicity 24,25,26 .…”

Synthesis and Self-Assembly Properties of Bola-Amphiphilic Glycosylated Lipopeptide-Type Supramolecular Hydrogels Showing Colour Changes Along with Gel–Sol Transition

“…The lipopeptides are a class of molecules with one or more lipid chains attached to a short peptide. Recently, self-assembled peptide-based nanomaterials have attracted significant attention, as functional materials [43][44][45][46][47][48][49]. Short peptide-based amphiphiles have been studied as hydrogelators due to their ability to assemble into a large range of novel nanostructures and their rational design for various applications, such as molecular sensors, tissue engineering, and drug-delivery systems [50][51][52][53][54][55][56].…”

Fine structural tuning of the assembly of ECM peptide conjugates via slight sequence modifications

“…In our previous work, we conjugated short synthetic ELPs (peptides, rather than polypeptides) with short synthetic triple-helical CLP domains and have shown that the association of the CLP triple helix substantially lowers the high inverse T t of the short peptidebased ELP domain into experimentally tractable and, in some cases, physiologically relevant temperature ranges (21,22). Subsequently, we demonstrated the formation of assembled ELP-CLP conjugates by tuning the hydrophobicity of ELP domains comprising (VPGXG) 4 , in which the number of repeats equipped with phenylalanine (F) or tryptophan (W) residues in the X position was varied (23). In contrast to vesicle structures, these W-containing ELP-CLP conjugates formed nanoscale platelet morphologies under aqueous conditions.…”

“…The chemical structure, molecular geometry, and solvent conditions can be tuned to affect the size, shape, and interfacial curvature of peptide-containing assembled structures ( 1 , 2 ), and the development of systematic design rules for the manipulation of architectures via small changes in sequence would offer substantial opportunities to expand their use ( 2 , 3 ). Stimuli-responsive domains have been incorporated that can undergo substantial property changes in response to small external changes in their environment, with triggers such as temperature, pH, and solvent ( 1 , 3 ); thermoresponsiveness is perhaps the most widely used owing to its ease of application ( 4 ), and the fact that peptide conformations such as helix, β turn, and coiled-coils can be manipulated by temperature ( 2 ). Accordingly, stimuli-responsive peptide-amphiphilic copolymers have demonstrated significant promise as drug carriers ( 4 , 5 ).…”

“…Stimuli-responsive domains have been incorporated that can undergo substantial property changes in response to small external changes in their environment, with triggers such as temperature, pH, and solvent ( 1 , 3 ); thermoresponsiveness is perhaps the most widely used owing to its ease of application ( 4 ), and the fact that peptide conformations such as helix, β turn, and coiled-coils can be manipulated by temperature ( 2 ). Accordingly, stimuli-responsive peptide-amphiphilic copolymers have demonstrated significant promise as drug carriers ( 4 , 5 ).…”