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Conformational dependence of integrin-binding peptides derived from homologous loop regions in the laminin α chains.
Journal of Peptide Science ( IF 2.1 ) Pub Date : 2020-09-03 , DOI: 10.1002/psc.3284
Masaya Ishikawa 1 , Keisuke Hamada 1 , Yuji Yamada 1 , Jun Kumai 1 , Fumihiko Katagiri 1 , Yamato Kikkawa 1 , Motoyoshi Nomizu 1
Affiliation  

Laminin α chains (α1–α5 chains) are expressed in a tissue‐ and developmental stage‐specific manner and have diverse chain‐specific biological functions. Especially, laminin globular (LG) modules (LG1–LG5) located at the C‐terminus of the α chains play a critical role in the biological activities of laminins. Each LG module is composed of a 14‐stranded β‐sheet (A‐N) sandwich structure. We previously screened cell attachment activity of the loop regions between the E and F strands in the LG modules using 17 homologous peptides (EF peptides) and found that four active EF peptides bind to integrin α2β1. One of the four peptides, G4EF1 demonstrated improved cell attachment activity when cyclized. Here, we focused on the remaining three integrin α2β1‐binding EF peptides (G5EF1, G3EF3, and G5EF5) and analyzed the relationship between their peptide conformation and cell attachment activity. First, we determined their active core sequences and found that G5EF1z (IGLEIVDGKVLFHVNN), G3EF3z (LLVTLEDGHIALST), and G5EF5z (KVLTEQVL) are the core sequences. Cyclic peptides of the core sequences (cycloG5EF1z, cycloG3EF3z, and cycloG5EF5z) enhanced integrin‐mediated cell adhesion activity compared with their linear peptides. The results indicated that cell adhesion activity of the integrin α2β1‐binding EF peptides is conformation dependent and that the loop structure is critical for their activity. This suggests that conformation of the loop regions plays an important role for the activities of the LG modules.

中文翻译:

从层粘连蛋白α链中同源环区域衍生的整联蛋白结合肽的构象依赖性。

层粘连蛋白α链(α1–α5链)以组织和发育阶段特异性方式表达,并具有多种链特异性生物学功能。尤其是,位于α链C末端的层粘连蛋白球状(LG)模块(LG1-LG5)在层粘连蛋白的生物学活性中起关键作用。每个LG模块均由14链β-折叠(A-N)三明治结构组成。我们先前使用17个同源肽(EF肽)筛选了LG模块中E和F链之间的环区域的细胞附着活性,发现四个有活性的EF肽与整联蛋白α2β1结合。环化时,四种肽之一G4EF1表现出改善的细胞附着活性。在这里,我们重点介绍了其余三个结合整联蛋白α2β1的EF肽(G5EF1,G3EF3,和G5EF5),并分析了它们的肽构象与细胞附着活性之间的关系。首先,我们确定了它们的活跃核心序列,并发现G5EF1z(IGLEIVDGKVLFHVNN),G3EF3z(LLVTLEDGHIALST)和G5EF5z(KVLTEQVL)是核心序列。与线性序列相比,核心序列的环肽(cycloG5EF1z,cycloG3EF3z和cycloG5EF5z)增强了整合素介导的细胞粘附活性。结果表明,整合素α2β1结合的EF肽的细胞粘附活性是构象依赖性的,并且环结构对其活性至关重要。这表明环区域的构象对于LG模块的活动起着重要作用。G3EF3z(LLVTLEDGHIALST)和G5EF5z(KVLTEQVL)是核心序列。核心序列的环肽(cycloG5EF1z,cycloG3EF3z和cycloG5EF5z)与其线性肽相比,增强了整合素介导的细胞粘附活性。结果表明,整合素α2β1结合的EF肽的细胞粘附活性是构象依赖性的,并且环结构对其活性至关重要。这表明环区域的构象对于LG模块的活动起着重要作用。G3EF3z(LLVTLEDGHIALST)和G5EF5z(KVLTEQVL)是核心序列。核心序列的环肽(cycloG5EF1z,cycloG3EF3z和cycloG5EF5z)与其线性肽相比,增强了整合素介导的细胞粘附活性。结果表明,整合素α2β1结合的EF肽的细胞粘附活性是构象依赖性的,并且环结构对其活性至关重要。这表明环区域的构象对于LG模块的活动起着重要作用。结果表明,整合素α2β1结合的EF肽的细胞粘附活性是构象依赖性的,并且环结构对其活性至关重要。这表明环区域的构象对于LG模块的活动起着重要作用。结果表明,整合素α2β1结合的EF肽的细胞粘附活性是构象依赖性的,并且环结构对其活性至关重要。这表明环区域的构象对于LG模块的活动起着重要作用。
更新日期:2020-11-04
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