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Influence of silk-silica fusion protein design on silica condensation in vitro and cellular calcification

机译：丝二氧化硅融合蛋白设计对体外和细胞钙化二氧化硅缩合的影响

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Biomaterial design via genetic engineering can be utilized for the rational functionalization of proteins to promote biomaterial integration and tissue regeneration. Spider silk has been extensively studied for its biocompatibility, biodegradability and extraordinary material properties. As a protein-based biomaterial, recombinant DNA derived derivatives of spider silks have been modified with biomineralization domains which lead to silica deposition and potentially accelerated bone regeneration. However, the influence of the location of the R5 (SSKKSGSYSGSKGSKRRIL) silicifying domain fused with the spider silk protein sequence on the biosilicification process remains to be determined. Here we designed two silk-R5 fusion proteins that differed in the location of the R5 peptide, C- vs. N-terminus, where the spider silk domain consisted of a 15mer repeat of a 33 amino acid consensus sequence of the major ampullate dragline spidroin 1 from Nephila clavipes (SGRGGLGGQG AGAAAAAGGA GQGGYGGLGSQGT). The chemical, physical and silica deposition properties of these recombinant proteins were assessed and compared to a silk 15mer control without the R5 present. The location of the R5 peptide did not have a significant effect on wettability and surface energies, while the C-terminal location of the R5 promoted more controlled silica precipitation, suggesting differences in protein folding and possibly different access to charged amino acids that drive the silicification process. Further, cell compatibility in vitro, as well as the ability to promote human bone marrow derived mesenchymal stem cell (hMSC) differentiation were demonstrated for both variants of the fusion proteins.
机译：通过基因工程的生物材料设计可用于蛋白质的合理官能化以促进生物材料整合和组织再生。蜘蛛丝已广泛研究了其生物相容性，生物分解性和非凡的材料特性。作为一种基于蛋白质的生物材料，已经用生物茂化结构域改变了蜘蛛丝网的重组DNA衍生物，其导致二氧化硅沉积和潜在加速的骨再生。然而，R5（SskksgsysgskgskRRRIL）硅化域与蜘蛛丝蛋白序列融合在生物纤米过程中的位置的影响仍然确定。在这里，我们设计了两种丝绸R5融合蛋白，其在R5肽的位置，C-vs.n-末端，其中蜘蛛丝结构域由蜘蛛丝域组成的，其具有主要的Ampullate Drawline Spidroin的33氨基酸共有序列的15mer重复1来自Nephila Clavipes（SGRGGLGGQG AGAAAAAGGA GQGGYGGLGSQGT）。评估这些重组蛋白的化学，物理和二氧化硅沉积特性，并与丝绸15mer控制进行比较，而没有R5存在。 R5肽的位置对润湿性和表面能没有显着影响，而R5的C末端位置促进了更受控的二氧化硅沉淀，表明蛋白质折叠的差异，并且可能不同于驱动硅化的带电氨基酸的差异过程。此外，对融合蛋白的两个变体证明了体外细胞相容性以及促进人骨髓衍生的间充质干细胞（HMSC）分化的能力。

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  • 来源
    《RSC Advances》 |2016年第26期|共13页
  • 作者

    Plowright Robyn; Dinjaski Nina; Zhou Shun; Belton David J.; Kaplan David L.; Perry Carole C.;

  • 作者单位

    Nottingham Trent Univ Sch Sci &

    Technol Interdisciplinary Biomed Res Ctr Biomol &

    Mat Interface Res Grp Clifton Lane Nottingham NG11 8NS England;

    Tufts Univ Dept Biomed Engn 4 Colby St Medford MA 02155 USA;

    Tufts Univ Dept Biomed Engn 4 Colby St Medford MA 02155 USA;

    Nottingham Trent Univ Sch Sci &

    Technol Interdisciplinary Biomed Res Ctr Biomol &

    Mat Interface Res Grp Clifton Lane Nottingham NG11 8NS England;

    Tufts Univ Dept Biomed Engn 4 Colby St Medford MA 02155 USA;

    Nottingham Trent Univ Sch Sci &

    Technol Interdisciplinary Biomed Res Ctr Biomol &

    Mat Interface Res Grp Clifton Lane Nottingham NG11 8NS England;

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