The scorpion venom Heterometrus fulvipes was able to uncouple the state-4 respiration of rat liver mitochondria. The venom caused mitochondrial swelling and was found to be inhibitory to mitochondrial succinate and glutamate dehydrogenases. Bovine serum albumin was able to protect against mitochondrial swelling.
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Expanding the pharmacological profile of κ-hefutoxin 1 and analogues: A focus on the inhibitory effect on the oncogenic channel K10.1.
Peptides
December 2017
Toxicology and Pharmacology, KU Leuven, Campus Gasthuisberg O&N2, Herestraat 49, PO Box 922, 3000 Leuven, Belgium. Electronic address:
Peptide toxins, such as scorpion peptides, are interesting lead compounds in the search for novel drugs. In this paper, the focus is on the scorpion peptide κ-hefutoxin 1. This peptide displays a cysteine-stabilized helix-loop-helix fold (CSα/α) and is known to be a weak K1.
View Article and Find Full Text PDFSynthesis and characterization of amino acid deletion analogs of κ-hefutoxin 1, a scorpion toxin on potassium channels.
Toxicon
September 2013
Laboratory of Toxicology, University of Leuven-K.U. Leuven, Campus Gasthuisberg O&N2, Herestraat 49, P.O. Box 922, 3000 Leuven, Belgium.
Nine analogs of scorpion toxin peptide κ-hefutoxin 1 were synthesized by stepwise deletion of its amino acid residues. Disulfide bond pairings of the synthetic analogs were confirmed by enzymatic digestion followed by MALDI-TOF-MS measurements. Functional characterization shows that analogs in which N-terminal residues were deleted retained biological activity, whereas deletion of middle part residues resulted in loss of activity.
View Article and Find Full Text PDFCloning, sequence analysis and homology modeling of a novel phospholipase A2 from Heterometrus fulvipes (Indian black scorpion).
DNA Seq
June 2007
Department of Biophysics, All India Institute of Medical Sciences, Ansari Nagar, New Delhi 110 029, India.
We report the cloning and sequencing of group III phospholipaseA(2) from Heterometrus fulvipes (HfPLA(2)), Indian black scorpion. The cDNA sequence codes for the mature portion of the group PLA(2) of 103 amino acids. The sequence has 85% identity with Mesobuthus tamulus (Indian red scorpion) PLA(2) and a 40% identity with bee venom PLA(2) and human group III PLA(2).
View Article and Find Full Text PDFAssignment of voltage-gated potassium channel blocking activity to kappa-KTx1.3, a non-toxic homologue of kappa-hefutoxin-1, from Heterometrus spinifer venom.
Biochem Pharmacol
February 2005
Department of Neurobiology, Harvard Medical School, Boston, MA 02115, USA.
A new family of weak K(+) channel toxins (designated kappa-KTx) with a novel "bi-helical" scaffold has recently been characterized from Heterometrus fulvipes (Scorpionidae) venom. Based on the presence of the minimum functional dyad (Y5 and K19), kappa-hefutoxin-1 (kappa-KTx1.1) was investigated and found to block Kv 1.
View Article and Find Full Text PDFkappa-Hefutoxin1, a novel toxin from the scorpion Heterometrus fulvipes with unique structure and function. Importance of the functional diad in potassium channel selectivity.
J Biol Chem
August 2002
Venom and Toxin Research Programme, Faculty of Medicine, National University of Singapore, 4 Medical Dr., Singapore 117597, Singapore.
An important and exciting challenge in the postgenomic era is to understand the functions of newly discovered proteins based on their structures. The main thrust is to find the common structural motifs that contribute to specific functions. Using this premise, here we report the purification, solution NMR, and functional characterization of a novel class of weak potassium channel toxins from the venom of the scorpion Heterometrus fulvipes.
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