Dissecting the Activity of Catechins as Incomplete Aldose Reductase Differential Inhibitors through Kinetic and Computational Approaches Article Swipe
Francesco Balestri
,
Giulio Poli
,
Lucia Piazza
,
Mario Cappiello
,
Roberta Moschini
,
Giovanni Signore
,
Tiziano Tuccinardi
,
Umberto Mura
,
Antonella Del Corso
·
YOU?
·
· 2022
· Open Access
·
· DOI: https://doi.org/10.3390/biology11091324
YOU?
·
· 2022
· Open Access
·
· DOI: https://doi.org/10.3390/biology11091324
The inhibition of aldose reductase is considered as a strategy to counteract the onset of both diabetic complications, upon the block of glucose conversion in the polyol pathway, and inflammation, upon the block of 3-glutathionyl-4-hydroxynonenal reduction. To ameliorate the outcome of aldose reductase inhibition, minimizing the interference with the detoxifying role of the enzyme when acting on toxic aldehydes, “differential inhibitors”, i.e., molecules able to inhibit the enzyme depending on the substrate the enzyme is working on, has been proposed. Here we report the characterization of different catechin derivatives as aldose reductase differential inhibitors. The study, conducted through both a kinetic and a computational approach, highlights structural constraints of catechin derivatives relevant in order to affect aldose reductase activity. Gallocatechin gallate and catechin gallate emerged as differential inhibitors of aldose reductase able to preferentially affect aldoses and 3-glutathionyl-4-hydroxynonenal reduction with respect to 4-hydroxynonenal reduction. Moreover, the results highlight how, in the case of aldose reductase, a substrate may affect not only the model of action of an inhibitor, but also the degree of incompleteness of the inhibitory action, thus contributing to differential inhibitory phenomena.
Related Topics
Concepts
Aldose reductase
Aldehyde Reductase
Biochemistry
Enzyme
Catechin
Biology
Reductase
4-Hydroxynonenal
Aldose reductase inhibitor
Polyphenol
Antioxidant
Lipid peroxidation
Metadata
- Type
- article
- Language
- en
- Landing Page
- https://doi.org/10.3390/biology11091324
- https://www.mdpi.com/2079-7737/11/9/1324/pdf?version=1662543107
- OA Status
- gold
- Cited By
- 2
- References
- 46
- Related Works
- 10
- OpenAlex ID
- https://openalex.org/W4295122492
All OpenAlex metadata
Raw OpenAlex JSON
- OpenAlex ID
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https://openalex.org/W4295122492Canonical identifier for this work in OpenAlex
- DOI
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https://doi.org/10.3390/biology11091324Digital Object Identifier
- Title
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Dissecting the Activity of Catechins as Incomplete Aldose Reductase Differential Inhibitors through Kinetic and Computational ApproachesWork title
- Type
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articleOpenAlex work type
- Language
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enPrimary language
- Publication year
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2022Year of publication
- Publication date
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2022-09-06Full publication date if available
- Authors
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Francesco Balestri, Giulio Poli, Lucia Piazza, Mario Cappiello, Roberta Moschini, Giovanni Signore, Tiziano Tuccinardi, Umberto Mura, Antonella Del CorsoList of authors in order
- Landing page
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https://doi.org/10.3390/biology11091324Publisher landing page
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https://www.mdpi.com/2079-7737/11/9/1324/pdf?version=1662543107Direct link to full text PDF
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YesWhether a free full text is available
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goldOpen access status per OpenAlex
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https://www.mdpi.com/2079-7737/11/9/1324/pdf?version=1662543107Direct OA link when available
- Concepts
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Aldose reductase, Aldehyde Reductase, Biochemistry, Enzyme, Catechin, Biology, Reductase, 4-Hydroxynonenal, Aldose reductase inhibitor, Polyphenol, Antioxidant, Lipid peroxidationTop concepts (fields/topics) attached by OpenAlex
- Cited by
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2Total citation count in OpenAlex
- Citations by year (recent)
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2025: 1, 2023: 1Per-year citation counts (last 5 years)
- References (count)
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46Number of works referenced by this work
- Related works (count)
-
10Other works algorithmically related by OpenAlex
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