Recent advances in nanofibrous assemblies based on β‐sheet‐forming peptides for biomedical applications

Waku, Tsuyoshi; Tanaka, Naoki

doi:10.1002/pi.5195

Cited by 16 publications

(16 citation statements)

References 106 publications

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“…Finally, the KCK-CPT prodrug was converted to the active form by glutathione (GSH) in the cytoplasm, inducing apoptosis in the cancer cell. Waku and Tanaka showed that self-assembling peptide nanofibrils can be used as potential delivery agents for vaccines 410,411. Highly antigen-loaded nano-assemblies were formed by conjugating antigens to β-sheet-forming peptides.…”

Section: Various Applications Of Amyloid-based Hybrid Nanomaterialsmentioning

confidence: 99%

Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology

et al. 2017

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Self-assembled peptide and protein amyloid nanostructures have traditionally been considered only as pathological aggregates implicated in human neurodegenerative diseases. In more recent times, these nanostructures have found interesting applications as advanced materials in biomedicine, tissue engineering, renewable energy, environmental science, nanotechnology and material science, to name only a few fields. In all these applications, the final function depends on: (i) the specific mechanisms of protein aggregation, (ii) the hierarchical structure of the protein and peptide amyloids from the atomistic to mesoscopic length scales and (iii) the physical properties of the amyloids in the context of their surrounding environment (biological or artificial). In this review, we will discuss recent progress made in the field of functional and artificial amyloids and highlight connections between protein/peptide folding, unfolding and aggregation mechanisms, with the resulting amyloid structure and functionality. We also highlight current advances in the design and synthesis of amyloid-based biological and functional materials and identify new potential fields in which amyloid-based structures promise new breakthroughs.

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Section: Various Applications Of Amyloid-based Hybrid Nanomaterialsmentioning

confidence: 99%

Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology

et al. 2017

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“…β -Sheet peptides have a high propensity to self-assemble in aqueous solutions and have thus been the focus of intense study as supramolecular materials. 27,116–118 Amyloid aggregates are an example of β -sheet assemblies that have been of special interest due to their relevance to protein folding disorders. 2,119,120 These materials have inspired the development of engineered β -sheet aggregates, which tend to be one-dimensional fibrils or nanoribbons that lack functional cytotoxicity and exhibit useful emergent properties that notably include the formation of entangled hydrogel networks.…”

Section: β-Sheet Peptidesmentioning

confidence: 99%

Multicomponent peptide assemblies

2018

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Self-assembled peptide nanostructures have been increasingly exploited as functional materials for applications in biomedicine and energy. The emergent properties of these nanomaterials determine the applications for which they can be exploited. It has recently been appreciated that nanomaterials composed of multicomponent coassembled peptides often display unique emergent properties that have the potential to dramatically expand the functional utility of peptide-based materials. This review presents recent efforts in the development of multicomponent peptide assemblies. The discussion includes multicomponent assemblies derived from short low molecular weight peptides, peptide amphiphiles, coiled coil peptides, collagen, and β-sheet peptides. The design, structure, emergent properties, and applications for these multicomponent assemblies are presented in order to illustrate the potential of these formulations as sophisticated next-generation bio-inspired materials.

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“…The development of biomaterials derived from self‐assembled peptides is of great current interest due to biomedical applications including controlled release drug delivery, vaccine development, tissue engineering, and wound healing . Amphipathic peptides that consist of alternating hydrophobic and hydrophilic amino acids are a privileged class of peptide that readily self‐assembles into β‐sheet bilayer nanoribbons that share the basic characteristics of cross‐β amyloid assemblies (Figure ) .…”

Section: Introductionmentioning

confidence: 99%

Balancing hydrophobicity and sequence pattern to influence self‐assembly of amphipathic peptides

2018

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Amphipathic peptides with alternating polar and nonpolar amino acid sequences efficiently selfassemble into functional b-sheet fibrils as long as the nonpolar residues have sufficient hydrophobicity. For example, the Ac-(FKFE) 2 -NH 2 peptide rapidly self-assembles into b-sheet bilayer nanoribbons, while Ac-(AKAE) 2 -NH 2 fails to self-assemble under similar conditions due to the significantly reduced hydrophobicity and b-sheet propensity of Ala relative to Phe. Herein, we systematically explore the effect of substituting only two of the four Ala residues at various positions in the Ac-(AKAE) 2 -NH 2 peptide with amino acids of increasing hydrophobicity, b-sheet potential, and surface area (including Phe, 1-naphthylalanine (1-Nal), 2-naphthylalanine (2-Nal), cyclohexylalanine (Cha), and pentafluorophenylalanine (F 5 -Phe)) on the self-assembly propensity of the resulting sequences. It was found that double Phe variants, regardless of the position of substitution, failed to self-assemble under the conditions used in this study. In contrast, all double 1-Nal and 2-Nal variants readily self-assembled, albeit at differing rates depending on the substitution patterns. To determine whether this was due to hydrophobicity or side chain surface area, we also prepared double Cha and F 5 -Phe variant peptides (both side chain groups are more hydrophobic than Phe). Each of these variants also underwent effective self-assembly, with the aromatic F 5 -Phe peptides doing so with greater efficiency. These findings provide insight into the role of amino acid hydrophobicity and sequence pattern on self-assembly proclivity of amphipathic peptides and on how targeted substitutions of nonpolar residues in these sequences can be exploited to tune the characteristics of the resulting self-assembled materials.hydrophobicity, peptide, self-assembly | I N TR ODU C TI ONThe development of biomaterials derived from self-assembled peptides is of great current interest due to biomedical applications including controlled release drug delivery, vaccine development, tissue engineering, and wound healing. Amphipathic peptides that consist of alternating hydrophobic and hydrophilic amino acids are a privileged class of peptide that readily self-assembles into b-sheet bilayer nanoribbons that share the basic characteristics of cross-b amyloid assemblies (Figure 1). [23][24][25][26][27][28][29][30] These bilayer nanoribbons effectively sequester all hydrophobic functionality to the bilayer interior, leaving hydrophilic groups exposed to solvent on the exterior face. [24,[31][32][33][34] As a result, these nanoribbons maintain high solubility in aqueous solvents, making them ideal materials for biological applications. Because of the high utility of this class of amphipathic peptide, they have been widely adopted as models to study the fundamental physicochemical basis of peptide self-assembly processes in order to facilitate the rational design of next-generation materials derived from self-assembled b-sheet peptides.[ [35][36][37][38][39]...

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Recent advances in nanofibrous assemblies based on β‐sheet‐forming peptides for biomedical applications

Cited by 16 publications

References 106 publications

Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology

Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology

Multicomponent peptide assemblies

Balancing hydrophobicity and sequence pattern to influence self‐assembly of amphipathic peptides

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