Amyloid management by chaperones: The mystery underlying protein oligomers’ dual functions

Arghavani, Payam; Pirhaghi, Mitra; Moosavi-Movahedi, Faezeh; Mamashli, Fatemeh; Hosseini, Elaheh; Moosavi-Movahedi, Ali Akbar

doi:10.1016/j.crstbi.2022.11.002

Cited by 10 publications

(7 citation statements)

References 40 publications

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“…Lag time is the ratelimiting step of nucleation-dependent aggregation processes at which early stage events including monomer activation (hydrolysis and unfolding in the case of SPI) and nucleation (oligomerization) occur. 43 Therefore, Cur not only accelerated early events of SPI aggregation but also increased the assembly rate in the exponential phase. As mentioned above, SPI aggregation is a hydrophobic driven process.…”

Section: ■ Experimental Sectionmentioning

confidence: 95%

In Situ Nanoencapsulation of Curcumin in Soy Protein Isolate Amyloid-like Aggregates for Enhanced Wound Healing

Arghavani,

Behjati Hosseini,

Moosavi-Movahedi

et al. 2024

ACS Appl. Mater. Interfaces

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The importance of amyloid nanofibrils made from food proteins is rising in diverse fields, such as biomedicine and food science. These protein nanofibrils (PNFs) serve as versatile and sustainable building blocks for biomaterials, characterized by their high β-sheet content and an ordered hydrogen bond network. These properties offer both stability and flexibility, along with an extreme aspect ratio and reactive functional groups. Plant-derived amyloid nanofibrils, such as soy protein isolate (SPI) PNFs, are increasingly favored due to their affordability and sustainability compared with animal proteins. This study aimed to explore the formation and application of SPI amyloid-like aggregates (SPIA) and their nanoencapsulation of curcumin (Cur) for biomedical purposes, particularly in wound healing. Under specific conditions of low pH and high temperature, SPIA formed, exhibited an amyloid nature, and successfully encapsulated Cur, thereby enhancing its stability and availability. Spectroscopic and microscopic analyses confirmed structural changes in SPIA upon the incorporation of Cur and the fabrication of SPIA@Cur. The obtained results indicate that in the presence of Cur, SPIA forms faster, attributed to accelerated SPI denaturation, an increased nucleation rate, and enhanced self-assembly facilitated by Cur's hydrophobic interactions and π−π stacking with SPI peptides. In vitro studies demonstrated the biocompatibility, biodegradability, and antioxidant properties of SPIA@Cur along with controlled release behavior. In vivo experiments in male Wistar rats revealed that both SPIA and SPIA@Cur significantly accelerate wound closure compared with untreated wounds, with SPIA@Cur showing slightly better efficacy. The histological analysis supported enhanced wound healing, indicating the potential of SPIA@Cur for biomedical applications.

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Section: ■ Experimental Sectionmentioning

confidence: 95%

In Situ Nanoencapsulation of Curcumin in Soy Protein Isolate Amyloid-like Aggregates for Enhanced Wound Healing

Arghavani,

Behjati Hosseini,

Moosavi-Movahedi

et al. 2024

ACS Appl. Mater. Interfaces

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“…164 Many studies have highlighted the role of soluble prefibrillar Aβ-oligomers as culprits that disrupt normal neuronal function and structure by damaging cellular components through various pathways. 165 Therefore, preventing Aβ aggregation and reducing its cellular concentrations are at the forefront of recent efforts to treat AD. 166 The following two subsections discuss the studies on CPPs and AD, which are summarized in Table 4.…”

Section: Application Of Cpps To Prevent Neuronal Degenerationmentioning

confidence: 99%

“…Current treatments are palliative and only modulates symptoms or at best slows the progression of disease. − Preventive or long-term strategies are currently lacking . Many studies have highlighted the role of soluble prefibrillar Aβ-oligomers as culprits that disrupt normal neuronal function and structure by damaging cellular components through various pathways . Therefore, preventing Aβ aggregation and reducing its cellular concentrations are at the forefront of recent efforts to treat AD .…”

Section: Application Of Cpps To Prevent Neuronal Degenerationmentioning

confidence: 99%

Cell-Penetrating Peptides: Promising Therapeutics and Drug-Delivery Systems for Neurodegenerative Diseases

Pirhaghi,

Mamashli,

Moosavi-Movahedi

et al. 2024

Mol. Pharmaceutics

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Currently, one of the most significant and rapidly growing unmet medical challenges is the treatment of neurodegenerative diseases such as Alzheimer's disease (AD) and Parkinson's disease (PD). This challenge encompasses the imperative development of efficacious therapeutic agents and overcoming the intricacies of the blood−brain barrier for successful drug delivery. Here we focus on the delivery aspect with particular emphasis on cell-penetrating peptides (CPPs), widely used in basic and translational research as they enhance drug delivery to challenging targets such as tissue and cellular compartments and thus increase therapeutic efficacy. The combination of CPPs with nanomaterials such as nanoparticles (NPs) improves the performance, accuracy, and stability of drug delivery and enables higher drug loads. Our review presents and discusses research that utilizes CPPs, either alone or in conjugation with NPs, to mitigate the pathogenic effects of neurodegenerative diseases with particular reference to AD and PD.

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“…These misfolded proteins can aggregate into amyloid brils characterized by a cross-linked β-sheet structure. Amyloid brils are implicated in a variety of diseases, including neurodegenerative disorders like Parkinson's, Alzheimer's, and Huntington's, as well as type 2 diabetes [5][6][7][8] . Albumin, a crucial water-soluble protein, is the major plasma protein synthesized in the liver and plays a signi cant role in transferring a broad spectrum of molecules, including water, salts, vitamins, hormones, and especially fatty acids, into the bloodstream 9 .…”

Section: Introductionmentioning

confidence: 99%

“…According to Gibbs free energy diagram reported against temperature 25 , elevating the temperature also results in protein conformational changes and triggers the unfolding or misfolding of protein. These changes in conformation expose buried hydrophobic regions of the protein 5 . Destabilized protein monomers of sticky hydrophobic patches nd each other, and their assembly fosters their propensity for aggregation 11,15 .…”

Section: Introductionmentioning

confidence: 99%

Unveiling the Forces Behind BSA Aggregation in a Microfluidic Chip

Haghparas,

Tabalvandani,

Arghavani

et al. 2024

Preprint

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Microfluidic chips are powerful tools for investigating protein aggregation. They can be used to study the effects of various variables on protein aggregation, including chemical and physical properties. This study investigated the aggregation of bovine serum albumin (BSA) in two different systems: a bulk system (vial) and a microfluidic chip in which BSA aggregation was induced successfully. Since BSA aggregation in bulk has been thoroughly investigated elsewhere, this study focused on elucidating the forces that drive BSA aggregation in a microfluidic chip designed explicitly for this purpose. This investigation employed a combination of experimental approaches, including biophysical and microscopic methods, and computational simulations using MATLAB and COMSOL Multiphysics. Obtained results revealed that heating provided the necessary energy for BSA's partial thermal unfolding from the onset. In the following, Brownian movement, space restriction, and a high molecular density within the microchannel cross-section contributed to forming clusters akin to the native BSA in the first few seconds. Subsequently, due to the further Brownian movement, intermolecular interactions, and hydrodynamic forces (including shear force), these clusters formed larger aggregates that deposited on the channel sidewalls and underwent a structural conversion, forming amyloid-like fibrillary aggregates within a few seconds.

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Amyloid management by chaperones: The mystery underlying protein oligomers’ dual functions

Cited by 10 publications

References 40 publications

In Situ Nanoencapsulation of Curcumin in Soy Protein Isolate Amyloid-like Aggregates for Enhanced Wound Healing

In Situ Nanoencapsulation of Curcumin in Soy Protein Isolate Amyloid-like Aggregates for Enhanced Wound Healing

Cell-Penetrating Peptides: Promising Therapeutics and Drug-Delivery Systems for Neurodegenerative Diseases

Unveiling the Forces Behind BSA Aggregation in a Microfluidic Chip

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