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• W3211117002 endingPage "100082" @default.
• W3211117002 startingPage "100082" @default.
• W3211117002 abstract "To mimic proteins, artificial designed self-assembling peptides (SAPs) that form diverse ordered nanostructures have been developed and served in biomedicine fields. In this review, we focus on four types of readily synthesized SAPs, including short aromatic peptides, peptide amphiphiles, amphipathic peptides, and surfactant-like peptides. Governed by multiple non-covalent interactions, sequence-coded and condition-altered self-organization of SAPs are presented, leading to the formation of versatile morphologies. The assembly of SAPs is an adaptable platform to incorporate with multiple bioactive motifs by chemical conjugation and physical encapsulation. These multifunctional SAPs-based nano-systems have demonstrated great potential to realize (i) combination therapies for synergetic anticancer effect, (ii) multimodal tumor imaging, (iii) antimicrobial materials that alleviate the drug-resistance problem, (iv) targeting and responsive hemostasis, and (v) active tissue regeneration. Future endeavor is encouraged to focus on the interactions between assemblies and cells, and the development of multi-component assemblies to facilitate the clinical translation of SAPs." @default.
• W3211117002 created "2021-11-08" @default.
• W3211117002 creator A5008167844 @default.
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• W3211117002 creator A5028859676 @default.
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• W3211117002 creator A5035551832 @default.
• W3211117002 creator A5044970833 @default.
• W3211117002 creator A5047120356 @default.
• W3211117002 creator A5050078481 @default.
• W3211117002 creator A5057760127 @default.
• W3211117002 creator A5083548371 @default.
• W3211117002 creator A5085632102 @default.
• W3211117002 date "2022-03-01" @default.
• W3211117002 modified "2023-10-06" @default.
• W3211117002 title "Supramolecular peptide nanostructures: Self-assembly and biomedical applications" @default.
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