Monitoring the Formation of Amyloid Oligomers Using Photoluminescence Anisotropy

Jiang, Bo; Aliyan, Amir; Cook, Nathan P.; Augustine, Andrea; Bhak, Ghibom; Maldonado, R.; McWilliams, Ashleigh D. Smith; Flores, Erick; Méndez, Natalia; Shahnawaz, Mohammad; Godoy, Fernando; Montenegro, Javier; Moreno-González, Inés; Martí, Ángel A.

doi:10.1021/jacs.9b06966

Cited by 51 publications

(60 citation statements)

References 27 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…For example, the Aβ-peptide labelled with a pyrene probe has been shown to sense the formation of oligomers by detecting a change in the anisotropy [ 116 ] (λex = 350 nm, λem = 460–500 nm (short live dimer or excimer) and 380–400 nm (monomer)). Additionally, a ruthenium polypyridyl complex (λex = 480 nm, λem = 605 nm) has been used to crosslink the formed Aβ-oligomers and follow the oligomerization process [ 117 ]. A similar approach labelling bovine serum albumin (BSA) with IAEDANS [ 118 ] was used to evaluate BSA aggregation.…”

Section: Fluorescence Spectroscopy Is a Versatile Tool For Evaluatmentioning

confidence: 99%

Evaluation of Peptide/Protein Self-Assembly and Aggregation by Spectroscopic Methods

2020

View full text Add to dashboard Cite

The self-assembly of proteins is an essential process for a variety of cellular functions including cell respiration, mobility and division. On the other hand, protein or peptide misfolding and aggregation is related to the development of Parkinson’s disease and Alzheimer’s disease, among other aggregopathies. As a consequence, significant research efforts are directed towards the understanding of this process. In this review, we are focused on the use of UV-Visible Absorption Spectroscopy, Fluorescence Spectroscopy and Circular Dichroism to evaluate the self-organization of proteins and peptides in solution. These spectroscopic techniques are commonly available in most chemistry and biochemistry research laboratories, and together they are a powerful approach for initial as well as routine evaluation of protein and peptide self-assembly and aggregation under different environmental stimulus. Furthermore, these spectroscopic techniques are even suitable for studying complex systems like those in the food industry or pharmaceutical formulations, providing an overall idea of the folding, self-assembly, and aggregation processes, which is challenging to obtain with high-resolution methods. Here, we compiled and discussed selected examples, together with our results and those that helped us better to understand the process of protein and peptide aggregation. We put particular emphasis on the basic description of the methods as well as on the experimental considerations needed to obtain meaningful information, to help those who are just getting into this exciting area of research. Moreover, this review is particularly useful to those out of the field who would like to improve reproducibility in their cellular and biomedical experiments, especially while working with peptide and protein systems as an external stimulus. Our final aim is to show the power of these low-resolution techniques to improve our understanding of the self-assembly of peptides and proteins and translate this fundamental knowledge in biomedical research or food applications.

show abstract

Section: Fluorescence Spectroscopy Is a Versatile Tool For Evaluatmentioning

confidence: 99%

Evaluation of Peptide/Protein Self-Assembly and Aggregation by Spectroscopic Methods

2020

View full text Add to dashboard Cite

show abstract

“…Finally, we used TEM analysis to determine the inhibitory effect of CUR-Fe 3 O 4 @CDs on the ultrastructural properties of assembled Aβ aggregates (Jiang et al, 2019). The Aβ 42 solution was incubated for 72 h to obtain abundant Aβ 42 fibrils.…”

Section: Effect Of Cur-fe 3 O 4 @Cds On Aβ 42 Aggregationmentioning

confidence: 99%

A Novel Nanosystem Realizing Curcumin Delivery Based on Fe3O4@Carbon Dots Nanocomposite for Alzheimer’s Disease Therapy

Kuang

Zhang

Xiong

et al. 2020

Front. Bioeng. Biotechnol.

View full text Add to dashboard Cite

Alzheimer’s disease (AD) is the most common neurodegenerative disease, which seriously affects human health but lacks effective treatment methods. Amyloid β (Aβ) aggregates are considered a possible target for AD treatment. Evidence is increasingly showing that curcumin (CUR) can partly protect cells from Aβ-mediated neurotoxicity by inhibiting Aβ aggregation. However, the efficiency of targeted cellular uptake and bioavailability of CUR is very low due to its poor stability and water-solubility. In order to better improve the cell uptake efficiency and bioavailability of CUR and reduce the cytotoxicity of high-dose CUR, a novel CUR delivery system for AD therapy has been constructed based on the employment of the Fe3O4@carbon dots nanocomposite (Fe3O4@CDs) as the carrier. CUR-Fe3O4@CDs have a strong affinity toward Aβ and effectively inhibit extracellular Aβ fibrillation. In addition, CUR-Fe3O4@CDs can inhibit the production of reactive oxygen species (ROS) mediated by Aβ fibrils and the corresponding neurotoxicity in PC12 cells. More importantly, it can restore nerve damage and maintained neuronal morphology. These results indicate that the application of CUR-Fe3O4@CDs provides a promising platform for the treatment of AD.

show abstract

“…On the other hand, the intrinsic blue/green photoluminescence recently associated to amyloid and amyloid-like structures has brought to the investigation of peptide and protein fibrils as fluorescent sources for monitoring the in vitro kinetics of aggregation (Liu et al, 2015;Gao et al, 2019). These photoluminescent materials (including peptide films and fibers), opportunely engineered, were evaluated as constituents for the development of integrated optoelectronic systems or waveguiding tools (Bo et al, 2019;. Moreover, the chemical access, the biocompatibility and the high loading capacity of both hydrophobic and hydrophilic drugs displayed by these peptide and protein nanostructures make them appealing tools for drug delivery applications (Stie et al, 2020).…”

Section: Other Applications Of Protein and Peptide Based Materials Wimentioning

confidence: 99%

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

Balasco

Diaferia

Morelli

et al. 2021

Front. Bioeng. Biotechnol.

View full text Add to dashboard Cite

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.

show abstract

Monitoring the Formation of Amyloid Oligomers Using Photoluminescence Anisotropy

Cited by 51 publications

References 27 publications

Evaluation of Peptide/Protein Self-Assembly and Aggregation by Spectroscopic Methods

Evaluation of Peptide/Protein Self-Assembly and Aggregation by Spectroscopic Methods

A Novel Nanosystem Realizing Curcumin Delivery Based on Fe3O4@Carbon Dots Nanocomposite for Alzheimer’s Disease Therapy

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

Contact Info

Product

Resources

About