Institut für Physikalische Biologie, Heinrich-Heine-Universität, 40225, Düsseldorf, Germany; Institute of Complex Systems (ICS-6) Structural Biochemistry, Forschungszentrum Jülich, 52425, Jülich, Germany.
J Pept Sci. 2014 May;20(5):334-40. doi: 10.1002/psc.2618. Epub 2014 Feb 24.
We studied the interaction of the SH3 domain of Bin1 with a 15-mer peptide of HCV NS5A and show its potency to competitively displace a 15-mer human c-Myc fragment, which is a physiological ligand of Bin1, using NMR spectroscopy. Fluorescence spectroscopy and ITC were employed to determine the affinity of Bin1 SH3 to NS5A(347-361), yielding a submicromolar affinity to NS5A. Our study compares the binding dynamics and affinities of the relevant regions for binding of c-Myc and NS5A to Bin1 SH3. The result gives further insights into the potential role of NS5A in Bin1-mediated apoptosis.
我们研究了 Bin1 的 SH3 结构域与 HCV NS5A 的 15 肽之间的相互作用，并通过 NMR 光谱证明了其竞争性置换 Bin1 的生理配体——人类 c-Myc 15 肽片段的能力。荧光光谱法和 ITC 用于确定 Bin1 SH3 与 NS5A(347-361)的亲和力，结果表明 NS5A 的亲和力达到亚毫摩尔级。本研究比较了 Bin1 SH3 与 c-Myc 和 NS5A 结合的相关区域的结合动力学和亲和力。结果进一步揭示了 NS5A 在 Bin1 介导的细胞凋亡中的潜在作用。
