Dipyridamole for tracking amyloidogenic proteins aggregation and enhancing polyubiquitination

Laneri, Francesca; García‐Viñuales, Sara; Lanza, Valeria; Licciardello, Nadia; Milardi, Danilo; Sortino, Salvatore; Grasso, Giuseppe

doi:10.1016/j.abb.2022.109354

Cited by 3 publications

(1 citation statement)

References 29 publications

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“…The misfolding and aggregation of specific proteins are often associated with some pathological states named “conformational diseases” (Soto & Pritzkow, 2018). Understanding the biomolecular mechanisms triggering the misfolding and the subsequent aggregation of proteins is of paramount importance for tackling many diseases, including diabetes and Alzheimer's disease, among others (Laneri et al, 2022). Notably, insulin is a protein deeply involved in the development and management of diabetes and, for this reason, its structure (Weiss, 2009), folding (Hua, 2010; Liu et al, 2018), protease susceptibility (Farris et al, 2003; Tundo et al, 2017), oligomerization and fibrillation (Nettleton et al, 2000; Zingale et al, 2023a), as well as interactions with different metal ions also involved in diabetes (Carpenter & Wilcox, 2014; Gavrilova et al, 2014; Kant et al, 2021; Lisi et al, 2014), have been widely investigated with a variety of experimental approaches.…”

Section: Introductionmentioning

confidence: 99%

Detection of insulin oligomeric forms by a novel surface plasmon resonance‐diffusion coefficient based approach

Calcagno,

Perina,

Zingale

et al. 2024

Protein Science

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Insulin is commonly used to treat diabetes and undergoes aggregation at the site of repeated injections in diabetic patients. Moreover, aggregation is also observed during its industrial production and transport and should be avoided to preserve its bioavailability to correctly adjust glucose levels in diabetic patients. However, monitoring the effect of various parameters (pH, protein concentration, metal ions, etc.) on the insulin aggregation and oligomerization state is very challenging. In this work, we have applied a novel Surface Plasmon Resonance (SPR)‐based experimental approach to insulin solutions at various experimental conditions, monitoring how its diffusion coefficient is affected by pH and the presence of metal ions (copper and zinc) with unprecedented sensitivity, precision, and reproducibility. The reported SPR method, hereby applied to a protein for the first time, besides giving insight into the insulin oligomerization and aggregation phenomena, proved to be very robust for determining the diffusion coefficient of any biomolecule. A theoretical background is given together with the software description, specially designed to fit the experimental data. This new way of applying SPR represents an innovation in the bio‐sensing field and expanding the potentiality of commonly used SPR instruments well over the canonical investigation of biomolecular interactions.

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Section: Introductionmentioning

confidence: 99%

Detection of insulin oligomeric forms by a novel surface plasmon resonance‐diffusion coefficient based approach

Calcagno,

Perina,

Zingale

et al. 2024

Protein Science

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Carbon dots as a versatile tool to monitor insulin aggregation

et al. 2023

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The possibility to monitor peptide and protein aggregation is of paramount importance in the so-called conformational diseases, as the understanding of many physiological pathways, as well as pathological processes involved in the development of such diseases, depends very much on the actual possibility to monitor biomolecule oligomeric distribution and aggregation. In this work, we report a novel experimental method to monitor protein aggregation, based on the change of the fluorescent properties of carbon dots upon protein binding. The results obtained in the case of insulin with this newly proposed experimental approach are compared with those obtained with other common experimental techniques normally used for the same purpose (circular dichroism, DLS, PICUP and ThT fluorescence). The greatest advantage of the hereby presented methodology over all the other experimental methods considered is the possibility to monitor the initial stages of insulin aggregation under the different experimental conditions sampled and the absence of possible disturbances and/or molecular probes during the aggregation process. Graphical abstract

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Construction and study of blood purification membrane modified with PDE inhibitor: Investigation of antiplatelet activity and hemocompatibility

Fu,

Lei,

Chen

et al. 2024

Colloids and Surfaces B: Biointerfaces

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Dipyridamole for tracking amyloidogenic proteins aggregation and enhancing polyubiquitination

Cited by 3 publications

References 29 publications

Detection of insulin oligomeric forms by a novel surface plasmon resonance‐diffusion coefficient based approach

Detection of insulin oligomeric forms by a novel surface plasmon resonance‐diffusion coefficient based approach

Carbon dots as a versatile tool to monitor insulin aggregation

Construction and study of blood purification membrane modified with PDE inhibitor: Investigation of antiplatelet activity and hemocompatibility

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