Silver nanoparticles as inhibitors of insulin amyloid formation: A fluorescence study

Vus, Kateryna; Tarabara, Uliana; Danylenko, I. M.; Pirko, Ya. V.; Krupodorova, Tetiana; Yemets, А. І.; Blume, Ya. B.; Турченко, В. А.; Klymchuk, D. O.; Smertenko, Petro; Zhytniakivska, Olga; Trusova, Valeriya; Petrushenko, S. I.; Bogatyrenko, S. I.; Gorbenko, Galyna

doi:10.1016/j.molliq.2021.117508

Cited by 12 publications

(7 citation statements)

References 82 publications

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“…However, the details are unknown. 36,37 Therefore, the observations obtained in this study have suggested the possibility that such inhibitors work against amyloid intermediates via interacting with the surface.…”

Section: Proposed Schemes For the Structural Development Of Prefibril...mentioning

confidence: 67%

“…Though they usually work via binding to the native state, − some of them are also predicted to interact with amyloid intermediates. However, the details are unknown. , Therefore, the observations obtained in this study have suggested the possibility that such inhibitors work against amyloid intermediates via interacting with the surface.…”

Section: Discussionmentioning

confidence: 88%

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Tracking the Structural Development of Amyloid Precursors in the Insulin B Chain and the Inhibition Effect by Fibrinogen

et al. 2022

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Amyloid fibrils are abnormal protein aggregates associated with several amyloidoses and neurodegenerative diseases. Prefibrillar intermediates, which emerge before amyloid fibril formation, play an important role in structure formation. Therefore, to prevent fibril formation, the mechanisms underpinning the structural development of prefibrillar intermediates must be elucidated. An insulin-derived peptide, the insulin B chain, is known for its stable accumulation of prefibrillar intermediates. In this study, the structural development of B chain prefibrillar intermediates and their inhibition by fibrinogen (Fg) were monitored by transmission electron microscopy (TEM) and small-angle X-ray scattering (SAXS) combined with solid-state nuclear magnetic resonance spectroscopy (NMR) and size exclusion chromatography. TEM images obtained in a time-lapse manner demonstrated that prefibrillar intermediates were wavy rod-like structures emerging from initial non-rod-like aggregates, and their bundling was responsible for protofilament formation. Time-resolved SAXS revealed that the prefibrillar intermediates became thicker and longer as a function of time. Solid-state NMR measurement suggested a β-sheet formation around Ala14 residue was crucial for the structural conversion from prefibrillar intermediates to amyloid fibril. These observations suggested that prefibrillar intermediates serve as reaction fields for amyloid nucleation and its structural propagation. Time-resolved SAXS also demonstrated that Fg prevented elongation of the prefibrillar intermediates by forming specific complexes together, which implied that regulation of the length of prefibrillar intermediates upon Fg binding was the factor suppressing the prefibrillar intermediate elongation. The fibril formation mechanism and the inhibition strategy found in this study will be helpful in seeking appropriate methods against amyloid-related diseases.

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Section: Proposed Schemes For the Structural Development Of Prefibril...mentioning

confidence: 67%

Section: Discussionmentioning

confidence: 88%

Tracking the Structural Development of Amyloid Precursors in the Insulin B Chain and the Inhibition Effect by Fibrinogen

et al. 2022

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“…Nanomaterials offer unique properties that arise from working at the nanoscale and are often used in medicine to provide a qualitative leap in therapy [ 61 ]. Among nanoparticles (NPs), those studied against insulin fibrillation include silicon NPs [ 62 ], ceria NPs [ 63 ], magnetite NPs [ 64 ], gold NPs [ 65 ], silver NPs [ 66 ], graphene oxide [ 67 ], organic NPs [ 68 ], carbon dots [ 69 , 70 , 71 ], and quantum dots [ 72 ]. Among molecules, there are glycopolymers [ 73 , 74 ], amphiphiles [ 75 ], aromatic molecules [ 76 ], polyphenols [ 6 , 77 , 78 ], vitamins [ 79 ], dyes [ 80 ], and various drugs [ 81 ].…”

Section: Peptide Inhibitors Of Insulin Fibrillationmentioning

confidence: 99%

Peptide Inhibitors of Insulin Fibrillation: Current and Future Challenges

Rosetti

Marchesan

2023

IJMS

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Amyloidoses include a large variety of local and systemic diseases that share the common feature of protein unfolding or refolding into amyloid fibrils. The most studied amyloids are those directly involved in neurodegenerative diseases, while others, such as those formed by insulin, are surprisingly far less studied. Insulin is a very important polypeptide that plays a variety of biological roles and, first and foremost, is at the basis of the therapy of diabetic patients. It is well-known that it can form fibrils at the site of injection, leading to inflammation and immune response, in addition to other side effects. In this concise review, we analyze the current knowledge on insulin fibrillation, with a focus on the development of peptide-based inhibitors, which are promising candidates for their biocompatibility but still pose challenges to their effective use in therapy.

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“…[16][17][18][19] Nanomaterials with varying physicochemical characteristics can affect protein structure and function. The inhibitory effects of various nanoparticles such as gold, 20,21 selenium, 22 silver, 23,24 and polymer-based nanoparticles [25][26][27][28] on the fibrillation process as a therapeutic method have been demonstrated in several investigations. 29,30 Several kinds of research have been performed to understand the function of various NPs in the protein fibrillation process, as well as the mechanisms by which NPs hinder or accelerate this process.…”

Section: Introductionmentioning

confidence: 99%

Inhibition of hen egg white lysozyme fibrillation by a self-assembled nanostructured lysozyme and graphene oxide conjugate

Mondal,

Paul

2023

New J. Chem.

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Silver nanoparticles as inhibitors of insulin amyloid formation: A fluorescence study

Cited by 12 publications

References 82 publications

Tracking the Structural Development of Amyloid Precursors in the Insulin B Chain and the Inhibition Effect by Fibrinogen

Tracking the Structural Development of Amyloid Precursors in the Insulin B Chain and the Inhibition Effect by Fibrinogen

Peptide Inhibitors of Insulin Fibrillation: Current and Future Challenges

Inhibition of hen egg white lysozyme fibrillation by a self-assembled nanostructured lysozyme and graphene oxide conjugate

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