Self‐Assembly of PEGylated Diphenylalanines into Photoluminescent Fibrillary Aggregates

Diaferia, Carlo; Roviello, Valentina; Morelli, Giancarlo; Accardo, Antonella

doi:10.1002/cphc.201900884

Cited by 26 publications

(29 citation statements)

References 67 publications

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“…Having a non-immunogenic and biocompatible profile, PEG bioconjugation (also referred to as PEGylation) finds applications in drug delivery [123], micelles, and liposome formulation [124], tissue engineering [125] and in pharmacokinetic profiles optimization [126]. Several hetero-peptides such as poly(γ-benzyl-l-aspartate) [127], [(AG)3EG]10 [128], DGRFFF [129], and (LELL) [130] have been PEGylated efficiently and fully characterized in their self-assembled states. An additional advantage of PEGylation is the possibility to modulate the water solubility and the structural organization of the final material.…”

Section: Fluorescence In Pegylated Films and Fibersmentioning

confidence: 99%

“…This result is strictly related to the hydrophobic/hydrophilic ratio in the polymer/peptide. The simplest PEGylated peptides described up to now are PEG2-FF and PEG6-FF ( Figure 11A) [130]. In these peptides, the F2 homodimer is derivatized at its N-terminus by two (PEG2) or six (PEG6) ethoxylic moieties.…”

Section: Fluorescence In Pegylated Films and Fibersmentioning

confidence: 99%

“…The proof-of-concept of a long-range FL probe was realized by testing conical PEG 24 -F6 fibers of 1.5 mm in length [130]. FL was excited by the 405 nm laser beam normally incident to the fiber axis, which exhibits quasi-white FL along the laser beam propagation (Figure 14).…”

Section: Spectral Range Attenuation Coefficient Characteristic Propagmentioning

confidence: 99%

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Fluorescence Phenomena in Amyloid and Amyloidogenic Bionanostructures

et al. 2020

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Nanoscale optical labeling is an advanced bioimaging tool. It is mostly based on fluorescence (FL) phenomena and enables the visualization of single biocells, bacteria, viruses, and biological tissues, providing monitoring of functional biosystems in vitro and in vivo, and the imaging-guided transportation of drug molecules. There is a variety of FL biolabels such as organic molecular dyes, genetically encoded fluorescent proteins (green fluorescent protein and homologs), semiconductor quantum dots, carbon dots, plasmonic metal gold-based nanostructures and more. In this review, a new generation of FL biolabels based on the recently found biophotonic effects of visible FL are described. This intrinsic FL phenomenon is observed in any peptide/protein materials folded into β-sheet secondary structures, irrespective of their composition, complexity, and origin. The FL effect has been observed both in natural amyloid fibrils, associated with neurodegenerative diseases (Alzheimer’s, Parkinson’s, and more), and diverse synthetic peptide/protein structures subjected to thermally induced biological refolding helix-like→β-sheet. This approach allowed us to develop a new generation of FL peptide/protein bionanodots radiating multicolor, tunable, visible FL, covering the entire visible spectrum in the range of 400–700 nm. Newly developed biocompatible nanoscale biomarkers are considered as a promising tool for emerging precise biomedicine and advanced medical nanotechnologies (high-resolution bioimaging, light diagnostics, therapy, optogenetics, and health monitoring).

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Section: Fluorescence In Pegylated Films and Fibersmentioning

confidence: 99%

Section: Fluorescence In Pegylated Films and Fibersmentioning

confidence: 99%

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Fluorescence Phenomena in Amyloid and Amyloidogenic Bionanostructures

et al. 2020

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“…Further structural information on nanogels was achieved by CD characterization. This spectroscopic methodology has been commonly applied to investigate the secondary structuration of proteins and peptide-based materials [ 36 , 37 , 38 ]. Indeed, secondary structural types, including α-helix, β-sheet, and random coil, generate distinctive CD spectra.…”

Section: Resultsmentioning

confidence: 99%

Stable Formulations of Peptide-Based Nanogels

et al. 2020

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Recently, nanogels have been identified as innovative formulations for enlarging the application of hydrogels (HGs) in the area of drug delivery or in diagnostic imaging. Nanogels are HGs-based aggregates with sizes in the range of nanometers and formulated in order to obtain injectable preparations. Regardless of the advantages offered by peptides in a hydrogel preparation, until now, only a few examples of peptide-based nanogels (PBNs) have been developed. Here, we describe the preparation of stable PBNs based on Fmoc-Phe-Phe-OH using three different methods, namely water/oil emulsion (W/O), top-down, and nanogelling in water. The effect of the hydrophilic–lipophilic balance (HLB) in the formulation was also evaluated in terms of size and stability. The resulting nanogels were found to encapsulate the anticancer drug doxorubicin, chosen as the model drug, with a drug loading comparable with those of the liposomes.

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“…Fmoc-FF-OH formed amyloid-like structures, nanofibers, and β-sheet-based fibrous-hydrogel, respectively (Reches and Gazit, 2005;Jayawarna et al, 2006;Mahler et al, 2006;Castelletto and Hamley, 2009;Diaferia et al, 2019b).…”

Section: Going Small: Oligopeptide-based Cross-β Assemblies For Biomamentioning

confidence: 99%

Amyloid-Like Aggregation in Diseases and Biomaterials: Osmosis of Structural Information

Balasco

Diaferia

Morelli

et al. 2021

Front. Bioeng. Biotechnol.

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The discovery that the polypeptide chain has a remarkable and intrinsic propensity to form amyloid-like aggregates endowed with an extraordinary stability is one of the most relevant breakthroughs of the last decades in both protein/peptide chemistry and structural biology. This observation has fundamental implications, as the formation of these assemblies is systematically associated with the insurgence of severe neurodegenerative diseases. Although the ability of proteins to form aggregates rich in cross-β structure has been highlighted by recent studies of structural biology, the determination of the underlying atomic models has required immense efforts and inventiveness. Interestingly, the progressive molecular and structural characterization of these assemblies has opened new perspectives in apparently unrelated fields. Indeed, the self-assembling through the cross-β structure has been exploited to generate innovative biomaterials endowed with promising mechanical and spectroscopic properties. Therefore, this structural motif has become the fil rouge connecting these diversified research areas. In the present review, we report a chronological recapitulation, also performing a survey of the structural content of the Protein Data Bank, of the milestones achieved over the years in the characterization of cross-β assemblies involved in the insurgence of neurodegenerative diseases. A particular emphasis is given to the very recent successful elucidation of amyloid-like aggregates characterized by remarkable molecular and structural complexities. We also review the state of the art of the structural characterization of cross-β based biomaterials by highlighting the benefits of the osmosis of information between these two research areas. Finally, we underline the new promising perspectives that recent successful characterizations of disease-related amyloid-like assemblies can open in the biomaterial field.

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Self‐Assembly of PEGylated Diphenylalanines into Photoluminescent Fibrillary Aggregates

Cited by 26 publications

References 67 publications

Fluorescence Phenomena in Amyloid and Amyloidogenic Bionanostructures

Fluorescence Phenomena in Amyloid and Amyloidogenic Bionanostructures

Stable Formulations of Peptide-Based Nanogels

Amyloid-Like Aggregation in Diseases and Biomaterials: Osmosis of Structural Information

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