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Steve Peigneur

Researcher at Katholieke Universiteit Leuven

Publications -  198
Citations -  3362

Steve Peigneur is an academic researcher from Katholieke Universiteit Leuven. The author has contributed to research in topics: Scorpion toxin & Venom. The author has an hindex of 27, co-authored 172 publications receiving 2553 citations. Previous affiliations of Steve Peigneur include Goethe University Frankfurt & Catholic University of Leuven.

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Neurotoxins and Their Binding Areas on Voltage-Gated Sodium Channels

TL;DR: This review focuses on the current status of research on neurotoxins acting on VGSC, their contribution to further unravel the structure and function of VGSC and their potential as novel lead compounds in drug development.
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Conotoxins Targeting Nicotinic Acetylcholine Receptors: An Overview

TL;DR: An overview of the knowledge the authors have today on the molecular pharmacology of conotoxins specifically interacting with nAChRs along with the structure–function relationship data is given.
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A bifunctional sea anemone peptide with Kunitz type protease and potassium channel inhibiting properties

TL;DR: This study demonstrates that APEKTx1 has the unique feature to combine the dual functionality of a potent and selective blocker of K(V)1.1 channels with that of a competitive inhibitor of trypsin.
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Targeting Cannabinoid Receptors: Current Status and Prospects of Natural Products.

TL;DR: It is expected that more novel cannabinoids will be discovered and forecasted as promising drug leads from diverse natural sources and species, such as animal venoms which constitute a true pharmacopeia of toxins modulating diverse targets, with astonishing affinity and selectivity.
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A natural point mutation changes both target selectivity and mechanism of action of sea anemone toxins

TL;DR: The target promiscuity of a family of sea anemone toxins thus far believed to be highly selective is described for the first time, and it is shown that the homologous toxins APETx1 and APetx2 display promiscuous properties since they are also capable of recognizing NaV channels with IC50 values of 31 nM and 114 nM, respectively, causing an inhibition of the sodium conductance without affecting the inactivation.