Human laminin‐511 (α5β1γ1) and its truncated protein, laminin‐511 E8 fragment, bind to integrin α6β1 and have been widely used for embryonic stem cell and induced pluripotent stem cell culture under feeder‐free conditions. In this study, we focused on human laminin α5 chain G domain, which is thought to be critical for the biological functions of laminin‐511, and screened its biologically active sequences using a synthetic peptide library. We synthesized 115 peptides (hA5G1‐hA5G115) covering the entire laminin α5 chain G domain and evaluated cell attachment activity using both the peptide‐coated plate and peptide‐chitosan matrix (peptide‐ChtM) assays. Seventeen peptides demonstrated cell attachment activity in the assays. Both hA5G18 and hA5G26‐coated plates and hA5G74‐ChtMs promoted integrin β1‐mediated cell attachment. These findings are useful for the study of molecular mechanisms of laminin‐511, and the active peptides have a potential for use as a molecular probe for cell adhesion receptors.

中文翻译：

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人层粘连蛋白α5G结构域中活性序列的鉴定。

人层粘连蛋白511（α5β1γ1）及其截短蛋白层粘连蛋白511 E8片段与整联蛋白α6β1结合，已广泛用于胚胎干细胞和无饲养层条件下诱导的多能干细胞培养。在这项研究中，我们专注于人层粘连蛋白α5链G结构域，该结构域对层粘连蛋白511的生物学功能至关重要，并使用合成肽库筛选了其生物活性序列。我们合成了115个肽段（hA5G1-hA5G115），覆盖了整个层粘连蛋白α5链G结构域，并使用肽包被的板和肽-壳聚糖基质（Peptide-ChtM）分析评估了细胞附着活性。在测定中有十七种肽表现出细胞附着活性。hA5G18和hA5G26包被的板以及hA5G74-ChtMs都促进整合素β1介导的细胞附着。