Solid-State NMR Characterization of Autofluorescent Fibrils Formed by the Elastin-Derived Peptide GVGVAGVG

Sharpe, Simon; Simonetti, Karen; Yau, Jason; Walsh, Patrick

doi:10.1021/bm101486s

Cited by 57 publications

(78 citation statements)

References 48 publications

(126 reference statements)

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“…The similarities in the lifetime and spectral signatures between the three species are remarkable, given their differences in amino acid sequence and aggregate morphology. These findings substantiate the hypothesis made previously, that the intrinsic fluorescence phenomenon is a generic property of the cross β-sheet arrangement in amyloid fibrils,[5, 7] and is likely related to the extensive arrangement of hydrogen-bond networks running along the fibril axis [6]. Crucially, we also show that intrinsic fluorescence permits individual fibrils to be imaged microscopically without any use of extrinsic labels.…”

Section: Resultssupporting

confidence: 92%

A Label‐Free, Quantitative Assay of Amyloid Fibril Growth Based on Intrinsic Fluorescence

et al. 2013

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Section: Resultssupporting

confidence: 92%

A Label‐Free, Quantitative Assay of Amyloid Fibril Growth Based on Intrinsic Fluorescence

et al. 2013

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“…We examined the aggregation of soluble NSF under various destabilizing conditions and found that the transformation of native silk from a disordered random coil to highly ordered‐rich β‐sheet‐rich structure is accompanied by the conformation appearance of a fluorescence signal a in the blue–green region of the visible spectrum, which features a long fluorescence lifetime ( Figure 1 ). Interestingly, the observed spectral and lifetime characteristics are very similar to those reported for amyloid fibrils, such as amyloid‐β, lysozyme, and α‐synuclein, suggesting that there is a common structural origin for the intrinsic fluorescence in NSF and in amyloid fibrils, independent on the presence of a chemical chromophore. Moreover, we show that aggregation of native silk produces a material with remarkably strong and stable fluorescence characteristics.…”

Section: Introductionsupporting

confidence: 72%

Biophotonics of Native Silk Fibrils

Shimanovich

Pinotsi

Shimanovich

et al. 2018

Macromolecular Bioscience

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is produced in multiple unrelated organ isms, [3] ranging from ants to spiders, with one of the most prevalent examples being the silkworm Bombyx mori (B. mori). The B. mori silkworm spins fibers from a precursor solution of liquid silk pro tein, stored in the animal's silk gland, and uses them to form a nonwoven composite cocoon protecting the animal during its further metamorphosis. [4] The silk fiber formation process exerts shear and elon gation stresses on a concentrated solu tion containing fibroin (up to 30% wt/vol) in the gland, causing soluble fibroin to denature and aggregate. [5] Many studies have been conducted on different types of silk, including the characterization of the structural nature of fibroin, [6,7] the aggre gation and fiber formation pathway, [8] as well as the mechanical and rheological properties of silk solutions and fibers. [9][10][11] These studies have shown that the mole cular architecture of fibrous silk assemblies and the associated irreversible aggregation processes are similar to those found for highly ordered amyloid fibrils. [12][13][14] As functional materials, silk fibroin (SF) fibers are of particular interest because of their Native Silk Fibrils Native silk fibroin (NSF) is a unique biomaterial with extraordinary mechanical and biochemical properties. These key characteristics are directly associated with the physical transformation of unstructured, soluble NSF into highly organized nano-and microscale fibrils rich in β-sheet content. Here, it is shown that this NSF fibrillation process is accompanied by the development of intrinsic fluorescence in the visible range, upon near-UV excitation, a phenomenon that has not been investigated in detail to date. Here, the optical and fluorescence characteristics of NSF fibrils are probed and a route for potential applications in the field of self-assembled optically active biomaterials and systems is explored.In particular, it is demonstrated that NSF can be structured into autofluorescent microcapsules with a controllable level of β-sheet content and fluorescence properties. Furthermore, a facile and efficient fabrication route that permits arbitrary patterns of NSF microcapsules to be deposited on substrates under ambient conditions is shown. The resulting fluorescent NSF patterns display a high level of photostability. These results demonstrate the potential of using native silk as a new class of biocompatible photonic material.

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“…But the fluorescent signal–to–noise ratio obtained for different crystals was variable and often not reproducible for the same crystals imaged at different times. Intrinsic blue–green fluorescence emission upon excitation with UVA light was previously observed for proteins in solution 33 , protein crystals and aggregates 43 , protein fibrils and matrix proteins 44, 45 , triethylamine and dendrimers containing amine/amide or imine groups ( 46 and references within). However, to the best of our knowledge, blue-green TPFE has not been used before to image protein crystals.…”

Section: Discussionmentioning

confidence: 79%

Imaging of Protein Crystals with Two-Photon Microscopy

et al. 2012

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Second–order non–linear optical imaging of chiral crystals (SONICC), that portrays second harmonic generation (SHG) by non–centrosymmetric crystals, is emerging as a powerful imaging technique for protein crystals in media opaque to visible light because of its high signal–to–noise ratio. Here we report the incorporation of both SONICC and two–photon excited fluorescence (TPEF) into one imaging system that allows visualization of crystals as small as ~10 μm in their longest dimension. Using this system, we then documented an inverse correlation between the level of symmetry in examined crystals and the intensity of their SHG. Moreover, because of blue-green TPEF exhibited by most tested protein crystals, we also could identify and image SHG–silent protein crystals. Our experimental data suggests that the TPEF in protein crystals is mainly caused by the oxidation of tryptophan residues. Additionally, we found that unspecific fluorescent dyes are able to bind to lysozyme crystals and enhance their detection by TPFE. We finally confirmed that the observed fluorescence was generated by a two-photon rather than a three-photon process. The capability for imaging small protein crystals in turbid or opaque media with non–damaging infrared light in a single system, makes the combination of SHG and intrinsic visible TPEF a powerful tool for non–destructive protein crystal identification and characterization during crystallization trials.

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Solid-State NMR Characterization of Autofluorescent Fibrils Formed by the Elastin-Derived Peptide GVGVAGVG

Cited by 57 publications

References 48 publications

A Label‐Free, Quantitative Assay of Amyloid Fibril Growth Based on Intrinsic Fluorescence

A Label‐Free, Quantitative Assay of Amyloid Fibril Growth Based on Intrinsic Fluorescence

Biophotonics of Native Silk Fibrils

Imaging of Protein Crystals with Two-Photon Microscopy

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