a-conotoxin ImI, a novel peptide which selectively targets neuronal nAChRs.McIntosh, J MYoshikami, DJohnson, D SMahe, ENielsen, D BRivier, J EGray, W ROlivera, B M
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A positional scan synthetic combinatorial library was constructed based on the three residues of the n-loop of z-conotoxin ImI to give a total of 10,648 possible combinations that were screened for functional activity in an α<sub>7</sub> nAChR Fluo-4/Ca<sup>2+</sup> assay, allowing ...
α-Conotoxin ImI incorporating stable cystathionine bridges maintains full potency and identical three-dimensional structure. The two disulfide bonds of α-conotoxin ImI, a peptide antagonist of the α7 nicotinic acetylcholine receptor (nAChR), were systematically replaced with isosteric redox-stable cystath...
Structural comparison of α-conotoxin BuIA with α4/7 conotoxins and α4/3 conotoxin ImI suggests that presence of the second helical turn portion of the two-turn helix motif in α4/7 and α4/4 conotoxins may be important for binding to the α3 and/or α6 subunit of nAChR....
to reject those solutions that were not in at least rough accordance with the available biochemical and mutagenesis data for long-chain alpha neurotoxins, and in the case of α-conotoxin GI, the complex was compared to the X-ray structure of the AChBP with conotoxin IMI (PDB code:2C9T)....
Oxidative folding of bicyclic conotoxins, such as α-ImI, has been traditionally achieved using two-step oxidation protocols with orthogonal protection on two native pairs of cysteines. In this work, two alternative oxidation protocols were explored: (1) the recently described one-pot oxidation of...
α-Conotoxin ImI is a 12-amino acid peptide, found in the venom of the marine snail Conus imperialis . This conotoxin is a selective antagonist of α7 nicotinic acetylcholine receptors. To produce biologically active α-ImI, disulfide bonds must be formed between Cys2–Cys8 and Cys3–Cys12...
To investigate if α-conotoxins interact with the nAChR in a similar manner, we built homology models of human α7 and α3β2 nAChRs, and performed docking simulations of α-conotoxins ImI, PnIB, PnIA and MII using the program GOLD. Docking revealed that α-conotoxins have a different ...
The structure of the dicarba analogue was similar to that of native α-ImI, with differences attributable to the different covalent geometry of the disulfide and dicarba bridges. Dicarba-α-ImI maintained inhibitory activity of nAChR comparable to that of native α-ImI in two in vitro assays. ...