ALPHA-CONOTOXINS, SMALL PEPTIDE PROBES OF NICOTINIC ACETYLCHOLINE-RECEPTORS
ALPHA-CONOTOXINS, SMALL PEPTIDE PROBES OF NICOTINIC ACETYLCHOLINE-RECEPTORS
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DOI：
10.1021/bi00102a034
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发表时间：
1991-09-24
期刊：
影响因子：
2.9
通讯作者：
OLIVERA, BM
中科院分区：
文献类型：
--
作者：
MYERS, RA;ZAFARALLA, GC;OLIVERA, BM
α-芋螺毒素是一种来自芋螺属海洋软体动物毒液的小肽家族，是烟碱乙酰胆碱受体的选择性蛇α-神经毒素竞争性拮抗剂。 一个新的α-芋螺毒素，SIA，已被纯化，测序和合成。用二价试剂交联和用α-芋螺毒素光亲和标记乙酰胆碱受体产生共价加合物。令人惊讶的是，与其他亚基的交联比与α-亚基的交联有效得多。 与受体的不同亚基的光活化交联的相对效率是光活化基团在毒素上的位置的函数。由于α-芋螺毒素的结构可以通过2D NMR解析[参见Pardi等（1989）Biochemistry 28，5494-5508;小林等（1989）Biochemistry 28，4853-4860]，该毒素家族应该提供一组新的配体用于以相当高的精度探测乙酰胆碱受体。
Alpha-Conotoxins, a family of small peptides from the venoms of the Conus marine mollusks, are selective, snake alpha-neurotoxin-competitive antagonists of the nicotinic acetylcholine receptor. A new alpha-conotoxin, SIA, has been purified, sequenced, and synthesized. Cross-linking with bivalent reagents and photoaffinity labeling of the acetylcholine receptor with alpha-conotoxin yield covalent adducts. Surprisingly, cross-linking to other subunits is considerably more efficient than to the alpha-subunit. The relative efficiency of photoactivatable cross-linking to different subunits of the receptor is a function of placement of the photoactivatable group on the toxin. Since the structures of alpha-conotoxins can be solved by 2D NMR [see Pardi et al. (1989) Biochemistry 28, 5494-5508; Kobayashi et al. (1989) Biochemistry 28, 4853-4860], this family of toxins should provide a set of new ligands for probing the acetylcholine receptor with considerable precision.