Amyloid-like Prep1 peptides exhibit reversible blue-green-red fluorescence <i>in vitro</i> and in living cells

Monti, Alessandra; Bruckmann, Chiara; Blasi, Francesco; Ruvo, Menotti; Vitagliano, Luigi; Doti, Nunzianna

doi:10.1039/d1cc01145f

Cited by 22 publications

(19 citation statements)

References 30 publications

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“…Notably, PEG24‐F6, which contains PEG moiety with a molecular weight around 1300 Da, is able to emit green fluorescence with a maximum at ∼530 nm upon excitation of the sample at λ exc ∼460 nm, a property that is rarely reported for self‐assembled proteins/peptide. [8b] Interestingly, solid state films prepared for deposition of self‐assembled peptide solutions were successfully used for the fabrication of passive optical waveguides, [18] thus suggesting wide applications in precision nanomedicine and integrated bio‐optics for these nanomaterials.…”

Section: Introductionmentioning

confidence: 99%

Fluorescence Emission of Self‐assembling Amyloid‐like Peptides: Solution versus Solid State

et al. 2021

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Analysis of the intrinsic UV-visible fluorescence exhibited by self-assembling amyloid-like peptides in solution and in solid the state highlights that their physical state has a profound impact on the optical properties. In the solid state, a linear dependence of the fluorescence emission peaks as a function of excitation wavelength is detected. On the contrary, an excitation-independent emission is observed in solution. The present findings constitute a valuable benchmark for current and future explanations of the fluorescence emission by amyloids.

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Section: Introductionmentioning

confidence: 99%

Fluorescence Emission of Self‐assembling Amyloid‐like Peptides: Solution versus Solid State

et al. 2021

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“…While GADD45γ retains a significant level of secondary structure at high temperature and is able to significantly regain the original folding upon cooling, GADD45α and GADD45β when heated form aggregated species enriched in β-structure, despite the remarkable content of α-helix in their native structures. Moreover, the spectroscopic characterization of these aggregates clearly indicates that they possess amyloid-like features as they bind the dye ThT and present the characteristic intrinsic UV/blue fluorescence emission [ 22 , 23 , 24 ]. As found for many amyloid-like species, the aggregates formed by GADD45α and GADD45β present a remarkable toxicity against SHSY-5Y and HepG2 cells.…”

Section: Discussionmentioning

confidence: 99%

Members of the GADD45 Protein Family Show Distinct Propensities to form Toxic Amyloid-Like Aggregates in Physiological Conditions

Smaldone

Caruso

Sandomenico

et al. 2021

IJMS

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The three members (GADD45α, GADD45β, and GADD45γ) of the growth arrest and DNA damage-inducible 45 (GADD45) protein family are involved in a myriad of diversified cellular functions. With the aim of unravelling analogies and differences, we performed comparative biochemical and biophysical analyses on the three proteins. The characterization and quantification of their binding to the MKK7 kinase, a validated functional partner of GADD45β, indicate that GADD45α and GADD45γ are strong interactors of the kinase. Despite their remarkable sequence similarity, the three proteins present rather distinct biophysical properties. Indeed, while GADD45β and GADD45γ are marginally stable at physiological temperatures, GADD45α presents the Tm value expected for a protein isolated from a mesophilic organism. Surprisingly, GADD45α and GADD45β, when heated, form high-molecular weight species that exhibit features (ThT binding and intrinsic label-free UV/visible fluorescence) proper of amyloid-like aggregates. Cell viability studies demonstrate that they are endowed with a remarkable toxicity against SHSY-5Y and HepG2 cells. The very uncommon property of GADD45β to form cytotoxic species in near-physiological conditions represents a puzzling finding with potential functional implications. Finally, the low stability and/or the propensity to form toxic species of GADD45 proteins constitute important features that should be considered in interpreting their many functions.

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“…Later, very similar intrinsic blue/green photoluminescence was observed in protein fibrils or nanostructures originated by self-assembly of short peptide sequences 14 – 16 . Very recent studies have further expanded these observations by showing that amyloid-like peptides and proteins are able to emit fluorescence in the near infrared region upon excitation at 650–700 nm 17 , 18 . This strong experimental evidence is somehow in contrast with the classical frame of fluorescence properties of proteins/peptides, which states that only the three aromatic amino acids (Phe, Tyr and Trp) are able to emit fluorescence in the far UV region 19 .…”

Section: Introductionmentioning

confidence: 92%

Solid-state optical properties of self-assembling amyloid-like peptides with different charged states at the terminal ends

Schiattarella

Diaferia

Gallo³

et al. 2022

Sci Rep

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The self-assembling of small peptides not only leads to the formation of intriguing nanoarchitectures, but also generates materials with unexpected functional properties. Oligopeptides can form amyloid-like cross-β assemblies that are able to emit intrinsic photoluminescence (PL), over the whole near-UV/visible range, whose origin is still largely debated. As proton transfer between the peptide chain termini within the assembly is one of the invoked interpretations of this phenomenon, we here evaluated the solid state PL properties of a series of self-assembled hexaphenylalanine peptides characterized by a different terminal charge state. Overall, our data indicate that the charge state of these peptides has a marginal role in the PL emission as all systems exhibit very similar multicolour PL associated with a violation of the Kasha’s rule. On the other hand, charged/uncharged ends occasionally produce differences in the quantum yields. The generality of these observations has been proven by extending these analyses to the Aβ16–21 peptide. Collectively, the present findings provide useful information for deciphering the code that links the spectroscopic properties of these assemblies to their structural/electronic features.

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Amyloid-like Prep1 peptides exhibit reversible blue-green-red fluorescence in vitro and in living cells

Abstract: PREP1-based peptides form amyloid-like aggregates endowed with an intrinsic blue-green-red fluorescence with an unusual sharp maximum at 520 nm upon excitation with visible light in physiological conditions. The peptide PREP1[117-132],...

Cited by 22 publications

References 30 publications

Fluorescence Emission of Self‐assembling Amyloid‐like Peptides: Solution versus Solid State

Fluorescence Emission of Self‐assembling Amyloid‐like Peptides: Solution versus Solid State

Members of the GADD45 Protein Family Show Distinct Propensities to form Toxic Amyloid-Like Aggregates in Physiological Conditions

Solid-state optical properties of self-assembling amyloid-like peptides with different charged states at the terminal ends

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