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胶原蛋白-纤连蛋白复合凝胶的声学制备加速了微组织的形成。

Acoustic Fabrication of Collagen-Fibronectin Composite Gels Accelerates Microtissue Formation.

作者信息

Norris Emma G, Dalecki Diane, Hocking Denise C

机构信息

Department of Pharmacology and Physiology, University of Rochester, Rochester, NY 14642, USA.

Department of Biomedical Engineering, University of Rochester, Rochester, NY 14627, USA.

出版信息

Appl Sci (Basel). 2020 Apr 2;10(8). doi: 10.3390/app10082907. Epub 2020 Apr 23.

DOI:10.3390/app10082907
PMID:33604063
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7889010/
Abstract

Ultrasound can influence biological systems through several distinct acoustic mechanisms that can be manipulated by varying reaction conditions and acoustic exposure parameters. We recently reported a new ultrasound-based fabrication technology that exploits the ability of ultrasound to generate localized mechanical forces and thermal effects to control collagen fiber microstructure non-invasively. Exposing solutions of type I collagen to ultrasound during the period of microfibril assembly produced changes in collagen fiber structure and alignment, and increased the biological activity of the resultant collagen hydrogels. In the extracellular matrix, interactions between fibronectin and collagen fibrils influence the biological activity of both proteins. Thus, in the present study, we examined how addition of fibronectin to collagen solutions prior to ultrasound exposure affects protein organization and the biological activity of the composite hydrogels. Results indicate that ultrasound can alter the distribution of fibronectin within 3D hydrogels via thermal and non-thermal mechanisms to produce composite hydrogels that support accelerated microtissue formation. The use of acoustic energy to drive changes in protein conformation to functionalize biomaterials has much potential as a unique, non-invasive technology for tissue engineering and regenerative medicine.

摘要

超声可通过多种不同的声学机制影响生物系统,这些机制可通过改变反应条件和声学暴露参数来操控。我们最近报道了一种基于超声的新型制造技术,该技术利用超声产生局部机械力和热效应的能力,以非侵入方式控制胶原纤维的微观结构。在微原纤维组装期间,将I型胶原溶液暴露于超声下,会使胶原纤维结构和排列发生变化,并提高所得胶原水凝胶的生物活性。在细胞外基质中,纤连蛋白与胶原纤维之间的相互作用会影响这两种蛋白质的生物活性。因此,在本研究中,我们研究了在超声暴露之前向胶原溶液中添加纤连蛋白如何影响蛋白质组织以及复合水凝胶的生物活性。结果表明,超声可通过热机制和非热机制改变纤连蛋白在三维水凝胶中的分布,从而产生支持加速微组织形成的复合水凝胶。利用声能驱动蛋白质构象变化以使生物材料功能化,作为一种用于组织工程和再生医学的独特非侵入技术具有很大潜力。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6634/7889010/459c40a3bc1a/nihms-1653646-f0006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6634/7889010/127d4eec474d/nihms-1653646-f0007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6634/7889010/87846df5bf34/nihms-1653646-f0001.jpg
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https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6634/7889010/84148209b5b8/nihms-1653646-f0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6634/7889010/0876689f1235/nihms-1653646-f0004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6634/7889010/9a6e7e8b3209/nihms-1653646-f0005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6634/7889010/459c40a3bc1a/nihms-1653646-f0006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6634/7889010/127d4eec474d/nihms-1653646-f0007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6634/7889010/87846df5bf34/nihms-1653646-f0001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6634/7889010/d5855540ab25/nihms-1653646-f0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6634/7889010/84148209b5b8/nihms-1653646-f0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6634/7889010/0876689f1235/nihms-1653646-f0004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6634/7889010/9a6e7e8b3209/nihms-1653646-f0005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/6634/7889010/459c40a3bc1a/nihms-1653646-f0006.jpg

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本文引用的文献

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Mater Res Express. 2019 Dec;6(12). doi: 10.1088/2053-1591/ab597a. Epub 2019 Nov 29.
2
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Mater Today Bio. 2019 Jun;3. doi: 10.1016/j.mtbio.2019.100018. Epub 2019 Jul 22.
3
Publicly Reported Wound Healing Rates: The Fantasy and the Reality.公开报告的伤口愈合率:幻想与现实。
Adv Wound Care (New Rochelle). 2018 Mar 1;7(3):77-94. doi: 10.1089/wound.2017.0743.
4
Flow-Induced Crystallization of Collagen: A Potentially Critical Mechanism in Early Tissue Formation.胶原的流致结晶:早期组织形成中一个潜在的关键机制。
ACS Nano. 2016 May 24;10(5):5027-40. doi: 10.1021/acsnano.5b07756. Epub 2016 Apr 27.
5
Cooperative effects of fibronectin matrix assembly and initial cell-substrate adhesion strength in cellular self-assembly.纤连蛋白基质组装与细胞-底物初始黏附强度在细胞自组装中的协同作用。
Acta Biomater. 2016 Mar 1;32:198-209. doi: 10.1016/j.actbio.2015.12.032. Epub 2015 Dec 19.
6
Mechanical forces regulate the interactions of fibronectin and collagen I in extracellular matrix.机械力调节细胞外基质中纤连蛋白和I型胶原蛋白的相互作用。
Nat Commun. 2015 Aug 14;6:8026. doi: 10.1038/ncomms9026.
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Review of collagen I hydrogels for bioengineered tissue microenvironments: characterization of mechanics, structure, and transport.用于生物工程组织微环境的I型胶原蛋白水凝胶综述:力学、结构和传输特性
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