S-layer-streptavidin fusion proteins and S-layer-specific heteropolysaccharides as part of a biomolecular construction kit for application in nanobiotechnology
S-layer-streptavidin fusion proteins and S-layer-specific heteropolysaccharides as part of a biomolecular construction kit for application in nanobiotechnology
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DOI：
10.1016/j.mee.2006.01.109
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发表时间：
2006-04-01
影响因子：
2.3
通讯作者：
Sara, Margit
中科院分区：
文献类型：
--
作者：
Huber, Carina;Egelseer, Eva M.;Sara, Margit
结晶细菌细胞表面层（S 层）蛋白代表许多细菌和古细菌的最外层包膜成分。分离的 S 层蛋白经常表现出在固体支持物、朗缪尔脂质膜或脂质体上重结晶成单分子蛋白晶格的能力。许多 S 层蛋白特异性识别一种独特类型的次生细胞壁聚合物 (SCWP) 作为刚性细胞壁层的正确锚定结构。这就是为什么此类杂多糖被用作固体支持物的仿生连接体的原因，如果使用在最外表面掺入外来序列的S层融合蛋白进行重结晶以生成功能性单分子蛋白晶格，这一点尤其重要。后者目前被用作无标记检测系统的传感层，作为结合免疫球蛋白的亲和基质，或者在脂质体的情况下，作为新型靶向和递送系统。 (c) 2006 Elsevier B.V. 保留所有权利。
Crystalline bacterial cell surface layer (S-layer) proteins represent the outermost envelope component of many bacteria and archaea. Isolated S-layer proteins frequently show the ability to recrystallize into monomolecular protein lattices on solid supports, Langmuir lipid films, or liposomes. Many S-layer proteins specifically recognize a distinct type of secondary cell wall polymer (SCWP) as the proper anchoring structure to the rigid cell wall layer. This is the reason why such heteropolysaccharides were exploited as biomimetic linkers to solid supports, which is especially important if S-layer fusion proteins having a foreign sequence incorporated on the outermost surface are used for recrystallization to generate functional monomolecular protein lattices. The latter are currently being exploited as sensing layers for label free detection systems, as affinity matrices for binding immunoglobulins, or in the case of liposomes, as novel targeting and delivery systems. (c) 2006 Elsevier B.V. All rights reserved.