Incorporation of a decorin biomimetic enhances the mechanical properties of electrochemically aligned collagen threads.

Incorporation of a decorin biomimetic enhances the mechanical properties of electrochemically aligned collagen threads.
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DOI:
10.1016/j.actbio.2011.02.035
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发表时间:
2011-06
期刊:
影响因子:
9.7
通讯作者:
Akkus, Ozan
Akkus, Ozan
中科院分区:
工程技术1区
文献类型:
--
作者:
Kishore, Vipuil;Paderi, John E.;Akkus, Anna;Smith, Katie M.;Balachandran, Dave;Beaudoin, Stephen;Panitch, Alyssa;Akkus, Ozan

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胶原分子的取向各向异性对于富含胶原的组织的机械强度是不可或缺的。我们以前曾报道过一种新的方法来合成高度取向的电化学排列胶原(ELAC)线与自然肌腱的机械性能收敛。核心蛋白聚糖是一种富含亮氨酸的小分子蛋白聚糖(SLRP),可与纤维状胶原蛋白结合,并被认为可增强肌腱的力学性能。基于天然核心蛋白聚糖的结构,我们先前设计并合成了一种肽聚糖(DS-SILY),其在结构和功能上都模拟核心蛋白聚糖。在这项研究中,我们调查了DS-SILY的掺入对ELAC线程的机械性能和结构组织的影响。结果表明,以30:1(胶原:DS-SILY)的摩尔比添加DS-SILY显著提高了ELAC线的极限应力和极限应变。此外,差示扫描量热法显示,以30:1的摩尔比添加DS-SILY导致更热稳定的胶原结构。然而,以较高浓度(10:1胶原:DS-SILY)添加DS-SILY产生较弱的线,其机械性质与胶原对照线相当。透射发射显微镜显示,添加较高浓度(10:1)的DS-SILY导致胶原原纤维明显聚集。更重要的是,这些聚集体没有沿着ELAC的长轴排列,从而损害了材料的整体拉伸性能。我们的结论是,纳入最佳量的DS-SILY是一个很有前途的方法来合成机械能力的胶原蛋白为基础的生物材料的肌腱组织工程应用。
Orientational anisotropy of collagen molecules is integral for the mechanical strength of collagen-rich tissues. We have previously reported a novel methodology to synthesize highly oriented electrochemically aligned collagen (ELAC) threads with mechanical properties converging upon those of native tendon. Decorin, a small leucine rich proteoglycan (SLRP), binds to fibrillar collagen and has been suggested to enhance the mechanical properties of tendon. Based on the structure of natural decorin, we have previously designed and synthesized a peptidoglycan (DS-SILY) that mimics decorin both structurally and functionally. In this study, we investigated the effect of the incorporation of DS-SILY on the mechanical properties and structural organization of ELAC threads. The results indicated that the addition of DS-SILY at a molar ratio of 30:1 (Collagen:DS-SILY) significantly enhanced the ultimate stress and ultimate strain of the ELAC threads. Furthermore, differential scanning calorimetry revealed that the addition of DS-SILY at a molar ratio of 30:1 resulted in a more thermally stable collagen structure. However, addition of DS-SILY at a higher concentration (10:1 Collagen:DS-SILY) yielded weaker threads with mechanical properties comparable to collagen control threads. Transmission emission microscopy revealed that the addition of DS-SILY at a higher concentration (10:1) resulted in pronounced aggregation of collagen fibrils. More importantly, these aggregates were not aligned along the long axis of the ELAC thereby compromising on the overall tensile properties of the material. We conclude that incorporation of an optimal amount of DS-SILY is a promising approach to synthesize mechanically competent collagen based biomaterials for tendon tissue engineering applications.
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发表时间: 1997-10-01
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DOI: 10.1111/j.1432-1033.1973.tb02739.x
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期刊: EUROPEAN JOURNAL OF BIOCHEMISTRY
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