Results 151 to 160 of about 356,030 (194)

Antimicrobial Peptides From Scorpion Venoms

open access: yesToxicon, 2014
The need for new antimicrobial agents is becoming one of the most urgent requirements in modern medicine. The venoms of many different species are rich sources of biologically active components and various therapeutic agents have been characterized including antimicrobial peptides (AMPs).
Patrick L Harrison   +2 more
exaly   +3 more sources

Unique Diversity of the Venom Peptides From the Scorpion Androctonus bicolor Revealed by Transcriptomic and Proteomic Analysis

open access: yesJournal of Proteomics, 2015
Androctonus bicolor is one of the most poisonous scorpion species in the world. However, little has been known about the venom composition of the scorpion.
Feng Ge, Mingkun Yang, Xian-Chun Zeng
exaly   +2 more sources
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Scorpion Venom Peptides With No Disulfide Bridges: A Review

Peptides, 2014
Scorpion venoms are rich sources of biologically active peptides that are classified into disulfide-bridged peptides (DBPs) and non-disulfide-bridged peptides (NDBPs). DBPs are the main scorpion venom components responsible for the neurotoxic effects observed during scorpion envenomation as they usually target membrane bound ion channels of excitable ...
Ammar Almaaytah
exaly   +3 more sources

Genetic Mechanisms of Scorpion Venom Peptide Diversification

Toxicon, 2006
The diversity of scorpion venom peptides is well shown by the presence of about 400 such polypeptides with or without disulfide bonds. Scorpion toxins with disulfide bonds present a variety of sequence features and pharmacological functions by affecting different ion channels, while the venom peptides without disulfide bonds represent a new subfamily ...
Zhijian Cao, Yingliang Wu
exaly   +3 more sources

Scorpion Venom Peptides Without Disulfide Bridges

IUBMB Life, 2005
Several hundred disulfide-bridged neurotoxic peptides have been characterized from scorpion venom; however, only few scorpion venom peptides without disulfide bridges have been identified and characterized. These non-disulfide-bridged peptides (NDBPs) are a novel class of molecules because of their unique antimicrobial, immunological or cellular ...
Gerardo Corzo, Xian-Chun Zeng
exaly   +3 more sources

Bioactive Peptides From Scorpion Venoms: Therapeutic Scaffolds and Pharmacological Tools

Chinese Journal of Natural Medicines, 2023
Evolution and natural selection have endowed animal venoms, including scorpion venoms, with a wide range of pharmacological properties. Consequently, scorpions, their venoms, and/or their body parts have been used since time immemorial in traditional medicines, especially in Africa and Asia.
Ren Lai, Bing Yao, Lei Luo
exaly   +3 more sources

A Simple Protocol for Venom Peptide Barcoding in Scorpions

open access: yesEuPA Open Proteomics, 2014
AbstractScorpion venoms contain many species-specific peptides which target ion channels in cell membranes. Without harming the scorpions, these peptides can easily be extracted and detected by MALDI-TOF mass spectrometry. So far, only few studies compared the venom of different species solely for taxonomic purposes.
Reinhard Predel
exaly   +2 more sources

Scorpion Venom Peptides as a Potential Source for Human Drug Candidates

Protein and Peptide Letters, 2018
Scorpion venom is the most expensive and deadly venom with exciting medical prospects and having a potential as a source of drug candidates. A number of scorpion venom peptides have shown promising site specificity and are involved in the regulation of biological mechanisms.
Tariq Mahmood   +2 more
exaly   +3 more sources

Scorpion and spider venom peptides: Gene cloning and peptide expression

Toxicon, 2011
This communication reviews most of the important findings related to venom components isolated from scorpions and spiders, mainly by means of gene cloning and expression. Rather than revising results obtained by classical biochemical studies that report structure and function of venom components, here the emphasis is placed on cloning and ...
V, Quintero-Hernández   +6 more
openaire   +2 more sources

Inhibition of CFTR channels by a peptide toxin of scorpion venom

American Journal of Physiology-Cell Physiology, 2004
Peptide toxins have been valuable probes in efforts to identify amino acid residues that line the permeation pathway of cation-selective channels. However, no peptide toxins have been identified that interact with known anion-selective channels such as the cystic fibrosis transmembrane conductance regulator (CFTR).
Matthew D, Fuller   +4 more
openaire   +2 more sources

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