各向异性弯曲刚度与自发曲率的新月形曲率诱导蛋白的估算：基于系绳囊泡实验数据
Estimation of anisotropic bending rigidities and spontaneous curvatures of crescent curvature-inducing proteins from tethered-vesicle experimental data
AI总结：
本研究基于系绳囊泡实验数据，利用各向异性弯曲能量平均场理论估算 BAR 蛋白的弯曲刚度与自发曲率，发现各向异性模型能更好拟合 I-BAR 数据，而 N-BAR 的拟合偏差可能源于其簇集形成。
摘要：
Bin/amphiphysin/Rvs (BAR) 超家族蛋白具有新月形结合域，并沿该结构域轴弯曲生物膜。然而，其各向异性弯曲刚度和自发曲率尚未通过实验确定。在此，我们利用各向异性弯曲能量和取向依赖排除体积的平均场理论，从系绳囊泡上的结合蛋白密度估算这些值。蛋白密度对膜曲率的依赖曲线分别拟合至 C. Prevost 等人发表于 Nat. Commun. 6, 8529 (2015) 和 F.-C. Tsai 等人发表于 Soft Matter 17, 4254 (2021) 报道的 I-BAR 和 N-BAR 结构域的实验数据。对于 I-BAR 结构域，不同化学势的三条密度曲线均与单一各向异性弯曲能量参数集表现出极佳拟合。若改用经典各向同性弯曲能量，其中一条曲线可良好拟合，但其他曲线出现较大偏差。相比之下，对于 N-BAR 结构域，使用各向异性模型无法同时良好拟合两条曲线，尽管相比各向同性模型已有显著改善。该偏差可能暗示了 N-BAR 结构域的簇集形成。
英文摘要：
The Bin/amphiphysin/Rvs (BAR) superfamily proteins have a crescent binding domain and bend biomembranes along the domain axis. However, their anisotropic bending rigidities and spontaneous curvatures have not been experimentally determined. Here, we estimated these values from the bound protein densities on tethered vesicles using a mean-field theory of anisotropic bending energy and orientation-dependent excluded volume. The dependence curves of the protein density on the membrane curvature are fitted to the experimental data for the I-BAR and N-BAR domains reported by C. Prevost et al. Nat. Commun. 6, 8529 (2015) and F.-C. Tsai et al. Soft Matter 17, 4254 (2021), respectively. For the I-BAR domain, all three density curves of different chemical potentials exhibit excellent fits with a single parameter set of anisotropic bending energy. When the classical isotropic bending energy is used instead, one of the curves can be fitted well, but the others exhibit large deviations. In contrast, for the N-BAR domain, two curves are not well-fitted simultaneously using the anisotropic model, although it is significantly improved compared to the isotropic model. This deviation likely suggests a cluster formation of the N-BAR domains.
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