Advanced search
Publication Cover
Phosphorus, Sulfur, and Silicon and the Related Elements Volume 197, 2022 - Issue 5-6: ICPC-23: 23rd International Conference on Phosphorus Chemistry; Guest Editors:Professor Jozef Drabowicz; Professor Piotr Kiełbasiński and Professor Tomasz Cierpiał
Submit an article Journal homepage
295
Views
0
CrossRef citations to date
0
Altmetric
Reviews

Phosphinic acid-based enzyme inhibitors

Stamatia Vassilioua Laboratory of Organic Chemistry, Department of Chemistry, University of Athens, Athens, GreeceORCID Iconhttps://orcid.org/0000-0002-0734-6579View further author information
ORCID Icon,
Aikaterini Pagonia Laboratory of Organic Chemistry, Department of Chemistry, University of Athens, Athens, GreeceView further author information
,
Ewelina Węglarz-Tomczakb Department of Bioorganic Chemistry, Faculty of Chemistry, Wrocław University of Science and Technology, Wrocław, PolandORCID Iconhttps://orcid.org/0000-0001-8080-2801View further author information
ORCID Icon,
Michał Talmab Department of Bioorganic Chemistry, Faculty of Chemistry, Wrocław University of Science and Technology, Wrocław, PolandView further author information
,
Wojciech Taborb Department of Bioorganic Chemistry, Faculty of Chemistry, Wrocław University of Science and Technology, Wrocław, PolandView further author information
,
Agnieszka Grabowieckab Department of Bioorganic Chemistry, Faculty of Chemistry, Wrocław University of Science and Technology, Wrocław, PolandORCID Iconhttps://orcid.org/0000-0002-5825-0702View further author information
ORCID Icon,
Łukasz Berlickib Department of Bioorganic Chemistry, Faculty of Chemistry, Wrocław University of Science and Technology, Wrocław, PolandORCID Iconhttps://orcid.org/0000-0003-0318-4944View further author information
ORCID Icon &
Artur Muchab Department of Bioorganic Chemistry, Faculty of Chemistry, Wrocław University of Science and Technology, Wrocław, PolandCorrespondence[email protected]
ORCID Iconhttps://orcid.org/0000-0002-6421-1371View further author information
ORCID Icon show all
Pages 451-456 | Received 29 Oct 2021, Accepted 22 Nov 2021, Published online: 10 Dec 2021
 
Sample our Physical Sciences journals, sign in here to start your FREE access for 14 days

Abstract

The phosphinic acid functionality has emerged as an invaluable scaffold for the construction of biologically active compounds, in particular enzyme inhibitors. This article presents two examples of recent achievements in the preparation and application of phosphinic acids as ligands for hydrolases. Synthetic approaches to a dipeptide analog inhibitor of metalloaminopeptidases and a catechol-based inhibitor of urease are shown. The activity and mode of binding of phosphinic compounds to enzymes are further discussed.

Graphical Abstract

Disclosure statement

No potential competing interest was reported by the authors.

Additional information

Funding

The work is supported by the National Science Centre, Poland, Grant No. 2018/31/B/NZ6/02017 (to A.M.).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Order Reprints Request Corporate Permissions

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

Request Academic Permissions

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.

Related research

People also read lists articles that other readers of this article have read.

Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.

Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.