Generation of a quenched phosphonate activity-based probe for labelling the active KLK7 protease-Reference-Cited by-同舟云学术

Generation of a quenched phosphonate activity-based probe for labelling the active KLK7 protease

Published:2021 Issue:31 Volume:19 Page:6834-6841
ISSN:1477-0520
Container-title:Organic & Biomolecular Chemistry
language:en
Short-container-title:Org. Biomol. Chem.

Author:

Bisyris Evangelos¹^ORCID,Zingkou Eleni¹,Kordopati Golfo G.¹^ORCID,Matsoukas Minos¹^ORCID,Magriotis Plato A.¹^ORCID,Pampalakis Georgios²^ORCID,Sotiropoulou Georgia¹^ORCID

Affiliation:

1. Department of Pharmacy, School of Health Sciences, University of Patras, Rion-Patras, 265 04, Greece

2. Department of Pharmacognosy-Pharmacology, School of Pharmacy, Aristotle University of Thessaloniki, Thessaloniki, 541 24, Greece

Abstract

A mixed alkyl aryl phosphonate qABP for KLK7 was developed where the internally-quenching system is realeased upon binding of the qABP to the active enzyme.

Funder

European Regional Development Fund

General Secretariat for Research and Technology

Publisher

Royal Society of Chemistry (RSC)

Subject

Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2021/OB/D1OB01273H

Reference36 articles.

1. Degradation of Corneodesmosome Proteins by Two Serine Proteases of the Kallikrein Family, SCTE/KLK5/hK5 and SCCE/KLK7/hK7

2. A Potential Role for Multiple Tissue Kallikrein Serine Proteases in Epidermal Desquamation

3. Redirecting drug repositioning to discover innovative cosmeceuticals

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