Chiral effect on Aβ fibrillation from molecular-scale to nanoscale

Gao, Guanbin; Zhu, Guowei; Yu, Liangchong; Zhang, Ting; Liu, Xinglin; Zhang, Cheng; Zhou, Ling; Sun, Taolei

doi:10.1007/s12274-022-4303-9

Cited by 9 publications

(3 citation statements)

References 46 publications

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“…For both HSA and Lyz, l -QDs possess larger K D ′ than that of d -QDs, suggesting a weaker binding affinity between l -QDs and proteins. Similar chirality-dependent protein adsorption behavior was also observed for other NPs in previous studies, which is mostly caused by the restriction of nanoscale chiral interfaces to the relative location of linked groups (−COOH and −NH 2 groups). ,, When proteins with specific steric conformation adsorb to chiral surfaces, the restriction has a strong impact on the type and strength of interaction forces, similar to spatial resistance . In addition, we found that the interaction between Lyz and QDs is stronger than that of HSA, which is likely caused by their different surface charges.…”

Section: Resultssupporting

confidence: 83%

Chirality-Dependent Dynamic Evolution of the Protein Corona on the Surface of Quantum Dots

Qiao

Zhong

et al. 2022

ACS Appl. Mater. Interfaces

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Elucidating the biological behavior of engineered nanoparticles, for example, the protein corona, is important for the development of safe and efficient nanomedicine, but our current understanding is still limited due to its highly dynamic nature and lack of adequate analytical tools. In the present work, we demonstrate the establishment of a fluorescence resonance energy transfer (FRET)-based platform for monitoring the dynamic evolution behavior of the protein corona in complex biological media. With human serum albumin and lysozyme as the model serum proteins, the protein exchange process of the preformed corona on the surface of chiral quantum dots (QDs) upon feeding either individual protein or human serum was monitored in situ by FRET. Important parameters characterizing the evolution process of protein corona could be obtained upon quantitative analysis of FRET data. Further combining real-time FRET monitoring with gel electrophoresis experiments revealed that the nature of the protein initially adsorbed on the surface of QDs significantly affects the subsequent dynamic exchange behavior of the protein corona. Furthermore, our results also revealed that only a limited proportion of proteins are involved in the protein exchange, and the exchange process exhibits a significant dependence on the surface chirality of QDs. This work demonstrates the feasibility of FRET as a powerful tool to exploit the dynamic evolution process of the protein corona, which can provide theoretical guidance for further design of advanced nanomaterials for biomedical applications.

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Section: Resultssupporting

confidence: 83%

Chirality-Dependent Dynamic Evolution of the Protein Corona on the Surface of Quantum Dots

Qiao

Zhong

et al. 2022

ACS Appl. Mater. Interfaces

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“…92 Some other noticeable work which includes chiral phospholipid surface and chiral zinc sulfide surface were also conducted for exploring the role of the chiral surface in amyloid formation. 93,94 Thus, all these published works showed the role of chiral surface in understanding the amyloid formation, which later can be useful for designing different detection systems as well as for therapy. In the following section, different chiral nanomaterials used for the detection and inhibition of amyloid fibrils are discussed.…”

Section: Chiral Nanomaterial-mediated Amyloid Formationmentioning

confidence: 99%

Chiral nanomaterial-based approaches for diagnosis and treatment of protein-aggregated neurodiseases: current status and future opportunities

Pranav,

Bajpai,

Dwivedi

et al. 2024

J. Mater. Chem. B

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“…The fourth level is ‘object chirality’, which usually comes from the accumulation of helical single domains to form mesoscopic or macroscopic chiral objects. Many studies show that the chiral variations of amino acids are able to affect Aβ specificity and induce Aβ isomerization and epimerization, which are closely associated with AD dysfunction [ 55 , 56 ]. Therefore, the chirality strategy has garnered widespread attention in the design of amyloid inhibitors.…”

Section: Poms As Inhibitors Of Aβ Aggregationmentioning

confidence: 99%

Polyoxometalates: metallodrug agents for combating amyloid aggregation

Ma,

Liu,

Zhao

et al. 2024

National Science Review

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Alzheimer's disease (AD) is a devastating neurodegenerative disease that affects approximately 50 million people globally. The accumulation of amyloid-β (Aβ) plaques, a predominant pathological feature of AD, plays a crucial role in AD pathogenesis. In this respect, Aβ has been regarded as a highly promising therapeutic target for AD treatment. Polyoxometalates (POMs) are a novel class of metallodrugs being developed as modulators of Aβ aggregation, owing to their negative charge, polarity, and three-dimensional structure. Unlike traditional discrete inorganic complexes, POMs contain tens to hundreds of metal atoms, showcasing remarkable tunability and diversity in nuclearities, sizes, and shapes. The easily adjustable and structurally variable nature of POMs allows for their favorable interactions with Aβ. This mini-review presents a balanced overview of recent progress in using POMs to mitigate amyloidosis. Clear correlations between anti-amyloid activities and structural features of POMs are also elaborated in detail. Finally, we discuss the current challenges and future prospects of POMs in combating AD.

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Chiral effect on Aβ fibrillation from molecular-scale to nanoscale

Cited by 9 publications

References 46 publications

Chirality-Dependent Dynamic Evolution of the Protein Corona on the Surface of Quantum Dots

Chirality-Dependent Dynamic Evolution of the Protein Corona on the Surface of Quantum Dots

Chiral nanomaterial-based approaches for diagnosis and treatment of protein-aggregated neurodiseases: current status and future opportunities

Polyoxometalates: metallodrug agents for combating amyloid aggregation

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