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首页> 美国卫生研究院文献>other >Solid-State Nuclear Magnetic Resonance Measurements of HIV Fusion Peptide to Lipid Distances Reveal Intimate Contact of β Strand Peptide with Membranes and Close Proximity of the Ala-14 to Gly-16 Region with Lipid Headgroups
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Solid-State Nuclear Magnetic Resonance Measurements of HIV Fusion Peptide to Lipid Distances Reveal Intimate Contact of β Strand Peptide with Membranes and Close Proximity of the Ala-14 to Gly-16 Region with Lipid Headgroups

机译：HIV融合肽对脂质距离的固态核磁共振测量揭示了β链肽与膜的紧密接触以及具有脂质头基的Ala-14至Gly-16区域的紧密接近。

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Human immunodeficiency virus (HIV) infection begins with fusion between viral and host cell membranes and is catalyzed by the HIV gp41 fusion protein. The ~20 N-terminal apolar residues of gp41 are called the HIV fusion peptide (HFP), interact with the host cell membrane, and play a key role in fusion. In this study, the membrane location of peptides which contained the HFP sequence AVGIGALFLGFLGAAGSTMGARS was probed in samples containing either only phospholipids or phospholipids and cholesterol. Four HFPs were examined which each contained 13CO labeling at three sequential residues between G5 and G16. The 13CO chemical shifts indicated that HFP had predominant β strand conformation over the labeled residues in the samples. The internuclear distances between the HFP 13COs and the lipid 31Ps were measured using solid-state nuclear magnetic resonance rotational-echo double resonance experiments. The closest 13CO-31P distances of 5–6 Å were observed for HFP labeled between A14 and G16 and correlated with intimate association of β strand HFP and membranes. These results were confirmed with measurements using HFPs singly 13CO labeled at A6 or A14. To our knowledge, these data are the first measurements of distances between HIV fusion peptide nuclei and lipid P and qualitative models of membrane location of oligomeric β strand HFP are presented which are consistent with the experimental data. Observation of intimate contact between β strand HFP and membranes provides rationale for further investigation of the relationship between structure and fusion activity for this conformation.
机译：人类免疫缺陷病毒（HIV）感染始于病毒和宿主细胞膜之间的融合，并被HIV gp41融合蛋白催化。 gp41的〜20 N末端非极性残基被称为HIV融合肽（HFP），与宿主细胞膜相互作用，并在融合中起关键作用。在这项研究中，在仅包含磷脂或磷脂和胆固醇的样品中检测了包含HFP序列AVGIGALFLGFLGAAGSTMGARS的肽的膜位​​置。检查了四个HFP，每个HFP在G5和G16之间的三个连续残基处包含 13 CO标记。 13 CO化学位移表明，HFP在样品中的标记残基上具有显着的β链构象。利用固态核磁共振旋转回波双共振实验测量了HFP 13 COs与脂质 31 Ps之间的核间距。对于标记在A14和G16之间的HFP，观察到最接近的 13 CO- 31 P距离为5-6Å，并且与β链HFP和膜的紧密结合相关。通过使用分别标记为A6或A14的 13 CO的HFP的测量结果证实了这些结果。据我们所知，这些数据是HIV融合肽核与脂质P之间距离的首次测量，并提出了寡聚β链HFP膜定位的定性模型，与实验数据一致。 β链HFP与膜之间紧密接触的观察为进一步研究该构象的结构与融合活性之间的关系提供了理论依据。

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