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一类新型抗艾滋病毒药物:GAP31、DAPs 30和32。

A new class of anti-HIV agents: GAP31, DAPs 30 and 32.

作者信息

Lee-Huang S, Kung H F, Huang P L, Huang P L, Li B Q, Huang P, Huang H I, Chen H C

机构信息

Department of Biochemistry, New York University School of Medicine, NY 10016.

出版信息

FEBS Lett. 1991 Oct 7;291(1):139-44. doi: 10.1016/0014-5793(91)81122-o.

Abstract

Three inhibitors of human immunodeficiency virus (HIV) have been isolated and purified to homogeneity from Euphorbiaceae himalaya seeds (Gelonium multiflorum) and carnation leaves (Dianthus caryophyllus). These proteins, GAP 31 (Gelonium Anti-HIV Protein 31 kDa) and DAPs 30 and 32 (dianthus anti-HIV proteins, 30 and 32 kDa), inhibit HIV-1 infection and replication in a dose-dependent manner with little toxicity to target cells. The therapeutic indices of these compounds are in the order 10(4), suggesting that they may be clinically important agents in the treatment of AIDS. The N-terminal amino acid sequences of these proteins show little homology to those of previously described anti-HIV proteins. The structure-function features of these HIV inhibitors, based on the 40-60 amino acid residues of N-terminal sequences, are examined.

摘要

从大戟科喜马拉雅种子(多花巴豆)和康乃馨叶片(香石竹)中分离并纯化出三种人免疫缺陷病毒(HIV)抑制剂,使其达到同质。这些蛋白质,即GAP 31(巴豆抗HIV蛋白,31 kDa)以及DAPs 30和32(康乃馨抗HIV蛋白,30和32 kDa),以剂量依赖方式抑制HIV-1感染和复制,对靶细胞毒性很小。这些化合物的治疗指数约为10(4),表明它们可能是治疗艾滋病临床上的重要药物。这些蛋白质的N端氨基酸序列与先前描述的抗HIV蛋白质的序列几乎没有同源性。基于N端序列的40 - 60个氨基酸残基,对这些HIV抑制剂的结构-功能特征进行了研究。

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