{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,7]],"date-time":"2026-10-07T06:23:38Z","timestamp":1791354218077,"version":"4.3.1"},"reference-count":53,"publisher":"Wiley","issue":"4","license":[{"start":{"date-parts":[[2004,2,3]],"date-time":"2004-02-03T00:00:00Z","timestamp":1075766400000},"content-version":"vor","delay-in-days":6242,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Proteins"],"published-print":{"date-parts":[[1987,1]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Peptides corresponding to portions of loop 2 of snake venom curare\u2010mimetic neurotoxins and to a structually similar region of rabies virus glycoprotein were synthesized. Interaction of these peptides with purified <jats:italic>Torpedo<\/jats:italic> electric organ acetylcholine receptor was tested by measuring their ability to block the binding of <jats:sup>125<\/jats:sup>I\u2010labeled \u03b1\u2010bungarotoxin to the receptor. In addition, inhibition of \u03b1\u2010bungarotoxin binding to a 32\u2010residue synthetic peptide corresponding to positions 173\u2013204 of the \u03b1\u2010subunit was determined. Neurotoxin and glycoprotein peptides corresponding to toxin loop 2 inhibited labeled toxin binding to the receptor with IC<jats:sub>50<\/jats:sub> values comparable to those of nicotine and the competitive antagonist d\u2010tubocurarine and to the \u03b1\u2010subunit peptides with apparent affinities between those of d\u2010tubocurarine and \u03b1\u2010cobratoxin. Substitution of neurotoxin residue Arg37, the proposed counterpart of the quatenary ammonium of acetylcholine, with a negatively charged Glu residue reduced the apparent affinity about 10\u2010fold. Peptides containg the neutotoxin invarint residue Trp29 had 10\u2010 to 100\u2010fold higher affinites than peptides lacking this residue. These results demonstrate that relatively short synthetic peptides retain some of binding ability of the native protein from which they are derived, indicating that such peptides are useful in the study of proetin interactions. The ability of the peptides to compete \u03b1\u2010bungarotoxin binding to the receptor with apparent affinites comparable to those of other cholinergic ligands indicates that loop 2 of the neurotoxins and the strucually similar segment of the rabies virus glycoprotein act as recognition sites for the acetylcholine receptor. Invarient toxin residues Arg37 and Trp29 and their viral homologs play important, although not essential, roles in binding, possibly by interaction with complementary anionic and hydrophobic subsites on the acetylcholine receptor. The \u03b1\u2010subunit peptide most likely contains all of the determinants for binding of the toxin and glycoprotein peptides present on the \u03b1\u2010subunit, because these peptides bind to the 32\u2010residue \u03b1\u2010subunit peptides with the same or greater affinity as to the intact subunit.<\/jats:p>","DOI":"10.1002\/prot.340020406","type":"journal-article","created":{"date-parts":[[2005,5,27]],"date-time":"2005-05-27T23:21:54Z","timestamp":1117236114000},"page":"298-307","source":"Crossref","is-referenced-by-count":65,"title":["Synthetic peptides corresponding to sequences of snake venom neurotoxins and rabies virus glycoprotein bind to the nicotinic acetylcholine receptor"],"prefix":"10.1002","volume":"2","author":[{"given":"Thomas L.","family":"Lentz","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Edward","family":"Hawrot","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Paul T.","family":"Wilson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2004,2,3]]},"reference":[{"key":"e_1_2_1_2_2","doi-asserted-by":"publisher","DOI":"10.3109\/10409238309102792"},{"key":"e_1_2_1_3_2","doi-asserted-by":"publisher","DOI":"10.1007\/978-3-642-66913-2_5"},{"key":"e_1_2_1_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0074-7742(08)60085-9"},{"key":"e_1_2_1_5_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.77.5.2400"},{"key":"e_1_2_1_6_2","doi-asserted-by":"publisher","DOI":"10.1093\/protein\/1.1.37"},{"key":"e_1_2_1_7_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1432-1033.1986.tb10481.x"},{"key":"e_1_2_1_8_2","doi-asserted-by":"publisher","DOI":"10.1101\/SQB.1983.048.01.004"},{"key":"e_1_2_1_9_2","first-page":"710","article-title":"Structure and function of snake venom curarimimetic neurotoxins","volume":"14","author":"Tsernoglou D.","year":"1978","journal-title":"Mol. 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