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A synthetic all d-amino acid peptide corresponding to the N-terminal sequence of HIV-1 gp41 recognizes the wild-type fusion peptide in the membrane and inhibits HIV-1 envelope glycoprotein-mediated cell fusion

机译:对应于HIV-1 gp41 N端序列的合成全d氨基酸肽识别膜中的野生型融合肽并抑制HIV-1包膜糖蛋白介导的细胞融合

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摘要

Recent studies demonstrated that a synthetic fusion peptide of HIV-1 self-associates in phospholipid membranes and inhibits HIV-1 envelope glycoprotein-mediated cell fusion, presumably by interacting with the N-terminal domain of gp41 and forming inactive heteroaggregates [Kliger, Y., Aharoni, A., Rapaport, D., Jones, P., Blumenthal, R. & Shai, Y. (1997) J. Biol. Chem. 272, 13496–13505]. Here, we show that a synthetic all d-amino acid peptide corresponding to the N-terminal sequence of HIV-1 gp41 (D-WT) of HIV-1 associates with its enantiomeric wild-type fusion (WT) peptide in the membrane and inhibits cell fusion mediated by the HIV-1 envelope glycoprotein. D-WT does not inhibit cell fusion mediated by the HIV-2 envelope glycoprotein. WT and D-WT are equally potent in inducing membrane fusion. D-WT peptide but not WT peptide is resistant to proteolytic digestion. Structural analysis showed that the CD spectra of D-WT in trifluoroethanol/water is a mirror image of that of WT, and attenuated total reflectance–fourier transform infrared spectroscopy revealed similar structures and orientation for the two enantiomers in the membrane. The results reveal that the chirality of the synthetic peptide corresponding to the HIV-1 gp41 N-terminal sequence does not play a role in liposome fusion and that the peptides’ chirality is not necessarily required for peptide–peptide interaction within the membrane environment. Furthermore, studies along these lines may provide criteria to design protease-resistant therapeutic agents against HIV and other viruses.
机译:最近的研究表明,HIV-1的合成融合肽可在磷脂膜上自缔合,并抑制HIV-1包膜糖蛋白介导的细胞融合,大概是通过与gp41的N末端结构域相互作用并形成无活性的异质聚集体[Kliger,Y。 ,Aharoni,A.,Rapaport,D.,Jones,P.,Blumenthal,R。&Shai,Y。(1997)J.Biol.Chem.Soc。,66:1593-63。化学272,13496–13505]。在这里,我们显示对应于HIV-1的HIV-1 gp41(D-WT)N端序列的合成全d-氨基酸肽与膜中的对映体野生型融合(WT)肽缔合,抑制由HIV-1包膜糖蛋白介导的细胞融合。 D-WT不抑制HIV-2包膜糖蛋白介导的细胞融合。 WT和D-WT在诱导膜融合方面同样有效。 D-WT肽而不是WT肽对蛋白水解消化具有抗性。结构分析表明,D-WT在三氟乙醇/水中的CD光谱与WT的镜像相同,衰减的全反射-傅立叶变换红外光谱显示膜中两种对映异构体的结构和方向相似。结果表明,与HIV-1 gp41 N端序列相对应的合成肽的手性在脂质体融合中不起作用,并且在膜环境中肽与肽的相互作用不一定需要该肽的手性。此外,沿着这些思路的研究可能会为设计针对HIV和其他病毒的蛋白酶抗性治疗剂提供标准。

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