ArticleAnalytical and bioanalytical chemistry2022
An SPR-based method for Hill coefficient measurements: the case of insulin-degrading enzyme.
Article in Analytical and bioanalytical chemistry, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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5 citing papers in PubMed, 10 citations in OpenAlex.
- Label-free determination of diffusion coefficients at the nanoscale through modelling of the Surface Plasmon Resonance signal.PloS one · 2025Article
- Applications of Surface Plasmon Resonance for Advanced Studies Involving Nucleic Acids.RNA nanomed · 2024Article
- Highly toxic Aβ begets more Aβ.Neural regeneration research · 2024Article
- Detection of insulin oligomeric forms by a novel surface plasmon resonance-diffusion coefficient based approach.Protein science : a publication of the Protein Society · 2024Article
- In Silico Investigation of the Clinical Translatability of Competitive Clearance Glucose-Responsive Insulins.ACS pharmacology & translational science · 2023Article
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3 authors at 1 institution in 1 country.
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Abstract
Insulin-degrading enzyme (IDE) is a highly conserved zinc metallopeptidase and is capable to catalytically cleave several substrates besides insulin, playing a pivotal role in several different biochemical pathways. Although its mechanism of action has been widely investigated, many conundrums still remain, hindering the possibility to rationally design specific modulators which could have important therapeutical applications in several diseases such as diabetes and Alzheimer's disease. In this scenario, we have developed a novel surface plasmon resonance (SPR) method which allows for directly measuring the enzyme cooperativity for the binding of insulin in the presence of different IDE activity modulators: carnosine, ATP, and EDTA. Results indicate that both positive and negative modulations of the IDE activity can be correlated to an increase and a decrease of the measured Hill coefficient, respectively, giving a new insight into the IDE activity mechanism. The use of the IDE R767A mutant for which oligomerization is hindered confirmed that the positive allosteric modulation of IDE by carnosine is due to a change in the enzyme oligomeric state occurring also for the enzyme immobilized on the gold SPR chip.
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