{"refrec":{"BRefID":322986,"RR":"<b>Peigneur, S.; Devi, P.; Seldeslachts, A.; Ravichandran, S.; Quinton, L.; Tytgat, J.</b> (2019). Structure-function elucidation of a new α-conotoxin, MiIIA, from <i>Conus milneedwardsi</i>. <i>Mar. Drugs 17(9)</i>: 535. <a href=\"https://dx.doi.org/10.3390/md17090535\" target=\"_blank\">https://dx.doi.org/10.3390/md17090535</a>","BEntID":316457,"PublicFlag":1,"CheckedFlag":1,"wosflag":1,"vabbflag":0,"RefStringPartII":". <i>Mar. Drugs 17(9)</i>: 535. <a href=\"https://dx.doi.org/10.3390/md17090535\" target=\"_blank\">https://dx.doi.org/10.3390/md17090535</a>","DocTypID":8,"DocType":"Journal article","MarineFlag":1,"FreshFlag":0,"BrackishFlag":0,"TerrestrialFlag":0,"Authorstring":"Peigneur, S.; Devi, P.; Seldeslachts, A.; Ravichandran, S.; Quinton, L.; Tytgat, J.","OrigTitleTranslFlag":0,"Authorstringtrunc":"Peigneur, S. <i>et al.</i>","Englishabstract":"The a-Conotoxins are peptide toxins that are found in the venom of marine cone snails and they are potent antagonists of various subtypes of nicotinic acetylcholine receptors (nAChRs). Because nAChRs have an important role in regulating transmitter release, cell excitability, and neuronal integration, nAChR dysfunctions have been implicated in a variety of severe pathologies. We describe the isolation and characterization of α-conotoxin MilIA, the first conopeptide from the venom of <span class=\"html-italic\">Conus milneedwardsi.</span> The peptide was characterized by electrophysiological screening against several types of cloned nAChRs that were expressed in <span class=\"html-italic\">Xenopus laevis</span> oocytes. MilIA, which is a member of the α3/5 family, is an antagonist of muscle type nAChRs with a high selectivity for muscle versus neuronal subtype nAChRs. Several analogues were designed and investigated for their activity in order to determine the key epitopes of MilIA. Native MilIA and analogues both showed activity at the fetal muscle type nAChR. Two single mutations (Met9 and Asn10) allowed for MilIA to strongly discriminate between the two types of muscle nAChRs. Moreover, one analogue, MilIA [∆1,M2R, M9G, N10K, H11K], displayed a remarkable enhanced potency when compared to native peptide. The key residues that are responsible for switching between muscle and neuronal nAChRs preference were elucidated. Interestingly, the same analogue showed a preference for α9α10 nAChRs among the neuronal types.","AbstractOtherLang":null,"BibLvlCode":"AS","StandardTitle":"Structure-function elucidation of a new α-conotoxin, MiIIA, from <i>Conus milneedwardsi</i>","OrigTitleLangCode":"en","OrigTitleLangCodeExtended":"eng","OrigTitleLangID":15,"DateLastModified":{"date":"2026-04-21 01:32:51.519378","timezone_type":1,"timezone":"+02:00"},"UserAccessRight":null,"UserAccID":null,"AuthorKeywords":"cone snail toxins; conopeptide; alpha-conotoxin; drug development;electrophysiology; ion channel diseases; nicotinic acetylcholinereceptor","OtherDescriptors":null,"Notes":null,"AnaPub":2019,"MonPub":null,"DateUpdate":"2020-04-08","DateCreate":"2020-04-07","SecASFANote":null,"ConfID":null,"PeerRev":1,"VlizCoreFlag":1,"WoScode":"WOS:000487959700024","VABBcode":null,"OpenAcc":1,"DOI":"10.3390/md17090535"},"refs":null,"anarec":{"AnaID":322986,"PubliDate":2019,"Pagination":"535","XtraPublOfAnaID":null,"ISBN":null,"Volume":"17","Issue":"9","BRefMon":null,"BRefMonRR":null,"BRefXtra":null,"BRefXtraRR":null,"SerBRefID":113252,"SerRR":"Marine Drugs. Molecular Diversity Preservation International (MDPI): Basel.  ISSN 1660-3397; e-ISSN 1660-3397","StandardTitleSer":"Marine Drugs","ISSN":"1660-3397","AbbrevSer":"Mar. 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