Self-Assembling Peptides as Building Blocks of Functional Materials for Biomedical Applications

Fukunaga, Kazuto; Tsutsumi, Hiroshi; Mihara, Hisakazu

doi:10.1246/bcsj.20180293

Cited by 85 publications

(50 citation statements)

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“…[ 23,28–31 ] In biomedical technology, such optical waveguides are fabricated from natural and synthetic polymer and hydrogel biocompatible materials and used for drug‐delivering imaging, light‐controlled therapy, cell‐based sensing, and optogenetics. [ 29,32–35 ]…”

Section: Introductionmentioning

confidence: 99%

Long‐Range Fluorescence Propagation in Amyloidogenic β‐Sheet Films and Fibers

Apter

Fainberg

Handelman

et al. 2020

Advanced Optical Materials

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Newly developed PEGylated phenylalanine peptide derivatives (PEG‐F6) can self‐assemble to form hybrid multifunctional nanostructures of homogeneous thin polymer films and amyloid‐like fibers. Both adopt a β‐sheet architecture and acquire the unique properties of visible fluorescence (FL) found in β‐sheet amyloid fibrils also associated with neurodegenerative diseases. A new paradigm observed in PEG‐F6 amyloid‐like fibers is reported, which demonstrates unique FL and optical absorption (OA) covering the entire visible region. Despite the full overlap of the FL and OA spectra, the FL propagates for an unexpectedly large distance of hundreds of micrometers in these fibers. A new non‐waveguiding mechanism of FL light energy transfer in amyloidogenic fibers is proposed based on photon reabsorption theory. The discovered quasi‐white FL of PEG‐F6 β‐sheet amyloidogenic fibers and films consists of the newly observed green FL band along the known blue FL band. The proof‐of‐concept of long sub‐millimeter range FL propagation in specially grown amyloidogenic PEG‐F6 fiber‐photonic probes is reported. The results indicate that FL can propagate in nanoscale fibers and suggest biomedical applications for FL monitoring of disease‐related ultrathin amyloid fibrils and in integrated photonics for optogenetics.

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Section: Introductionmentioning

confidence: 99%

Long‐Range Fluorescence Propagation in Amyloidogenic β‐Sheet Films and Fibers

Apter

Fainberg

Handelman

et al. 2020

Advanced Optical Materials

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“…Silica nanostructures, along with other types of nanostructures, have long been studied for biomedical applications owing to their synthetic flexibilities, molecular specificities, multifunctionalities, and biocompatibilities. [ 19–24 ] Safety of the ultralarge pore mesoporous silica nanoparticles has not been a strong concern as amorphous silica is already approved as a food additive by the US Food and Drug Administration. [ 25 ] The scFv‐loaded, Aβ nanodepletors blocked Aβ self‐assembly, drastically decreased the amount of Aβ aggregates, and increased cell viability.…”

Section: Introductionmentioning

confidence: 99%

Silica Nanodepletors: Targeting and Clearing Alzheimer's β‐Amyloid Plaques

Jung

Chung

Wilton

et al. 2020

Adv Funct Materials

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Abnormal accumulation of β-amyloid (Aβ) peptide aggregates in the brain is a major hallmark of Alzheimer's disease (AD). Aβ aggregates interfere with neuronal communications, ultimately causing neuronal damage and brain atrophy. Much effort has been made to develop AD treatments that suppress Aβ aggregate formation, thereby attenuating Aβ-induced neurotoxicity. Here, the design of Aβ nanodepletors consisting of ultralarge mesoporous silica nanostructures and anti-Aβ single-chain variable fragments, with the goal of targeting and eliminating aggregative Aβ monomers, is reported. The Aβ nanodepletors impart a notable decline in Aβ aggregate formation, resulting in significant mitigation of Aβ-induced neurotoxicity in vitro. Furthermore, stereotaxic injections of Aβ nanodepletors into the brain of an AD mouse model system successfully suppress Aβ plaque formation in vivo up to ≈30%, suggesting that Aβ nanodepletors can serve as a promising antiamylodoisis material.aged 65 and older are living with AD, [4] which accounts for an estimated 60-80% of dementia.Accumulation of extracellular β-amyloid (Aβ) plaques and intracellular tau proteinderived neurofibrillary tangles are major hallmarks of Alzheimer-associated brain damages in AD patients. These features are being explored from the perspective of pathological diagnosis and clinical treatment of AD. [5,6] Aβ monomers, which are derived from the cleavage of amyloid precursor protein by βand γ-secretase, [7] assemble into toxic Aβ oligomers and aggregates having cross β-sheet-rich secondary structures that induce neuronal damages. [8][9][10][11] Ultimately, the self-assembly process leads to the deposition of amyloid plaques, a strong and stable network that is difficult to break. Hence, removing monomeric Aβ at the early stage of dementia is thought to be a promising strategy for slowing the progression of AD. [12][13][14][15][16] Here, we report an Aβ-depleting nanostructure (denoted hereafter as Aβ nanodepletors) that can selectively capture and clear Aβ peptide monomers in brain (Scheme 1).

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“…Moreover, the molecular hydrogel has the ability of self-delivery and could realize a higher local density at the target sites. The self-assembled molecules include drugs, 22 peptides, [23][24][25] sugar-based compounds, 26 and amino acid-derivatives, 27 which could work as both hydrogelator and active "drug". For example, Yang and his group 28 used two kinds of anti-inammatory molecules and a uranyl ion chelating ligand to form the supramolecular hydrogel.…”

Section: Introductionmentioning

confidence: 99%