Results 31 to 40 of about 186,549 (302)

Structure-Based Prototype Peptides Targeting the Pseudomonas aeruginosa Type VI Secretion System Effector as a Novel Antibacterial Strategy

open access: yesFrontiers in Cellular and Infection Microbiology, 2017
The type VI secretion system (T6SS) secretes numerous toxins for bacteria-bacteria competition. TplE is a newly identified trans-kingdom toxin secreted by the T6SS in Pseudomonas aeruginosa, while TplEi neutralizes the toxic effect of TplE to protect ...
Xiaopan Gao   +4 more
doaj   +1 more source

Structure of the voltage-gated potassium channel KV1.3: Insights into the inactivated conformation and binding to therapeutic leads

open access: yesChannels, 2023
The voltage-gated potassium channel KV1.3 is an important therapeutic target for the treatment of autoimmune and neuroinflammatory diseases. The recent structures of KV1.3, Shaker-IR (wild-type and inactivating W434F mutant) and an inactivating mutant of
K. George Chandy   +2 more
doaj   +1 more source

Cyclotides: Disulfide-rich peptide toxins in plants [PDF]

open access: yesToxicon, 2019
Cyclotides are a plant-derived family of peptides that comprise approximately 30 amino acid residues, a cyclic backbone and a cystine knot. Due to their unique structure, cyclotides are exceptionally stable to heat or proteolytic degradation and are tolerant to amino acid substitutions in their backbone loops between conserved cysteine residues.
Yen-Hua Huang   +2 more
openaire   +5 more sources

Assembling an arsenal, the scorpion way

open access: yesBMC Evolutionary Biology, 2008
Background For survival, scorpions depend on a wide array of short neurotoxic polypeptides. The venoms of scorpions from the most studied group, the Buthida, are a rich source of small, 23–78 amino acid-long peptides, well packed by either three or four ...
Mishmar Dan   +3 more
doaj   +1 more source

Scorpion Toxin, BmP01, Induces Pain by Targeting TRPV1 Channel

open access: yesToxins, 2015
The intense pain induced by scorpion sting is a frequent clinical manifestation. To date, there is no established protocol with significant efficacy to alleviate the pain induced by scorpion envenomation.
Md Abdul Hakim   +6 more
doaj   +1 more source

Peptide isolated from Cry1Ab16 toxin present in Bacillus thuringiensis: Synthesis and morphology data for layer-by-layer films studied by atomic force microscopy

open access: yesData in Brief, 2016
The peptide PcL342-354C was obtained from the Cry1Ab16 toxin present in Bacillus thuringiensis (“Computational Modeling Deduced Three Dimensional Structure of Cry1Ab16 Toxin from B. thuringiensis AC11” (Kashyap, 2012) [1]).
Alexandra Plácido   +5 more
doaj   +1 more source

A novel RRGW derived peptide is a promising inhibitor of BoNT/A

open access: yesJournal of Enzyme Inhibition and Medicinal Chemistry, 2023
Clostridium botulinum neurotoxin type A (BoNT/A) is one of the most potent biotoxins ever known. Its entry into neurons could block vesicle exocytosis to abolish the release of neurotransmitters from nerve terminals, thus leading to muscle paralysis ...
Wantong Ma   +10 more
doaj   +1 more source

Peptide-Conjugated Pterins as Inhibitors of Ricin Toxin A [PDF]

open access: yesJournal of Medicinal Chemistry, 2012
Several 7-peptide-substituted pterins were synthesized and tested as competitive active-site inhibitors of ricin toxin A (RTA). Focus began on dipeptide conjugates, and these results further guided the construction of several tripeptide conjugates. The binding of these compounds to RTA was studied via a luminescence-based kinetic assay, as well as ...
Ryota, Saito   +8 more
openaire   +2 more sources

Identification of a peptide motif that potently inhibits two functionally distinct subunits of Shiga toxin

open access: yesCommunications Biology, 2021
Watanabe-Takahashi, Tamada, Senda et al. identify a tetravalent peptide that inhibits Shiga toxin (Stx), a major virulence factor of enterohemorrhagic Escherichia coli, by targeting its receptor-binding.
Miho Watanabe-Takahashi   +8 more
doaj   +1 more source

Purification and Characterization of JZTx-14, a Potent Antagonist of Mammalian and Prokaryotic Voltage-Gated Sodium Channels

open access: yesToxins, 2018
Exploring the interaction of ligands with voltage-gated sodium channels (NaVs) has advanced our understanding of their pharmacology. Herein, we report the purification and characterization of a novel non-selective mammalian and bacterial NaVs toxin, JZTx-
Jie Zhang   +6 more
doaj   +1 more source

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