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首页> 外文期刊>Journal of biomedical materials research. Part B, Applied biomaterials. >Engineering integrin-specific surfaces with a triple-helical collagen-mimetic peptide
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Engineering integrin-specific surfaces with a triple-helical collagen-mimetic peptide

机译：用三螺旋胶原蛋白模拟肽工程化整联蛋白特异性表面

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摘要

Integrin-mediated cell adhesion to extracellular matrix proteins anchors cells and triggers signals that direct cell function. The integrin alpha _2 beta _1 recognizes the glycine-phenylalanine-hydroxyproline-glycine-glutamate-arginine (GFOGER) motif in residues 502-507 of the alpha _1(I) chain of type I collagen. Integrin recognition is entirely dependent on the triple-helical conformation of the ligand similar to that of native collagen. This study focuses on engineering alpha _2 beta _1 -specific bioadhesive surfaces by immobilizing a triple-helical collagen-mimetic peptide incorporating the GFOGER binding sequence onto model nonadhesive substrates. Circular dichroism spectroscopy verified that this peptide adopts a stable triple-helical conformation in solution. Passively adsorbed GFOGER-peptide exhibited dose-dependent HT1080 cell adhesion and spreading comparable to that observed on type I collagen. Subsequent antibody blocking conditions verified the involvement of integrin alpha _2 beta _1 in these adhesion events. Focal adhesion formation was observed by immunofluorescent staining for alpha _2 beta _1 and vinculin on MC3T3-E1 cells. Model functionalized surfaces then were engineered using three complementary peptide-tethering schemes. These peptide-functionalized substrates supported alpha _2 beta _1-mediated cell adhesion and focal adhesion assembly. Our results suggest that this peptide is active in an immobilized conformation and may be applied as a surface modification agent to promote alpha _2 beta _1-specific cell adhesion. Engineering surfaces that specifically target certain integrin-ligand interactions and signaling cascades provides a biomolecular strategy for optimizing cellular responses in biomaterials and tissue engineering applications.
机译：整联蛋白介导的细胞与细胞外基质蛋白的粘附锚定细胞并触发指导细胞功能的信号。整联蛋白α_2 beta _1识别I型胶原α_1（I）链的残基502-507中的甘氨酸-苯丙氨酸-羟脯氨酸-甘氨酸-谷氨酸-精氨酸（GFOGER）基序。整联蛋白识别完全取决于与天然胶原相似的配体的三螺旋构象。这项研究的重点是通过将掺入GFOGER结合序列的三螺旋胶原蛋白模拟肽固定在模型非粘附性基质上，从而工程化特定于α_2β_1的生物粘附表面。圆二色光谱证实该肽在溶液中采用稳定的三螺旋构象。被动吸附的GFOGER肽表现出剂量依赖性的HT1080细胞粘附和扩散，与I型胶原上观察到的相当。随后的抗体阻断条件验证了整合素alpha _2 beta _1参与了这些粘附事件。通过免疫荧光染色对MC3T3-E1细胞上的α_2β_1和纽蛋白进行了局部粘着形成。然后使用三种互补的肽链方案对模型功能化的表面进行工程设计。这些肽功能化的底物支持alpha _2 beta _1介导的细胞粘附和粘着大会。我们的结果表明，该肽具有固定构象的活性，可以用作表面修饰剂来促进α_2β_1特异性细胞粘附。专门针对某些整联蛋白-配体相互作用和信号级联反应的工程表面提供了一种生物分子策略，可优化生物材料和组织工程应用中的细胞反应。

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