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重组蜘蛛丝:前景与瓶颈

Recombinant Spider Silk: Promises and Bottlenecks.

作者信息

Ramezaniaghdam Maryam, Nahdi Nadia D, Reski Ralf

机构信息

Plant Biotechnology, Faculty of Biology, University of Freiburg, Freiburg, Germany.

Cluster of Excellence livMatS at FIT - Freiburg Center for Interactive Materials and Bioinspired Technologies, University of Freiburg, Freiburg, Germany.

出版信息

Front Bioeng Biotechnol. 2022 Mar 8;10:835637. doi: 10.3389/fbioe.2022.835637. eCollection 2022.

DOI:10.3389/fbioe.2022.835637
PMID:35350182
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8957953/
Abstract

Spider silk threads have exceptional mechanical properties such as toughness, elasticity and low density, which reach maximum values compared to other fibre materials. They are superior even compared to Kevlar and steel. These extraordinary properties stem from long length and specific protein structures. Spider silk proteins can consist of more than 20,000 amino acids. Polypeptide stretches account for more than 90% of the whole protein, and these domains can be repeated more than a hundred times. Each repeat unit has a specific function resulting in the final properties of the silk. These properties make them attractive for innovative material development for medical or technical products as well as cosmetics. However, with livestock breeding of spiders it is not possible to reach high volumes of silk due to the cannibalistic behaviour of these animals. In order to obtain spider silk proteins (spidroins) on a large scale, recombinant production is attempted in various expression systems such as plants, bacteria, yeasts, insects, silkworms, mammalian cells and animals. For viable large-scale production, cost-effective and efficient production systems are needed. This review describes the different types of spider silk, their proteins and structures and discusses the production of these difficult-to-express proteins in different host organisms with an emphasis on plant systems.

摘要

蜘蛛丝具有非凡的机械性能,如韧性、弹性和低密度,与其他纤维材料相比,这些性能达到了最大值。即使与凯夫拉尔纤维和钢铁相比,它们也更具优势。这些非凡的性能源于其长链长度和特定的蛋白质结构。蜘蛛丝蛋白可以由超过20000个氨基酸组成。多肽片段占整个蛋白质的90%以上,这些结构域可以重复一百多次。每个重复单元都有特定的功能,从而决定了蛛丝的最终性能。这些特性使其在医疗、技术产品以及化妆品等创新材料开发方面具有吸引力。然而,由于蜘蛛的同类相食行为,通过饲养蜘蛛无法获得大量的蛛丝。为了大规模获得蜘蛛丝蛋白(蛛丝蛋白),人们尝试在各种表达系统中进行重组生产,如植物、细菌、酵母、昆虫、家蚕、哺乳动物细胞和动物。为了实现可行的大规模生产,需要具有成本效益且高效的生产系统。本综述描述了不同类型的蜘蛛丝、它们的蛋白质和结构,并讨论了在不同宿主生物体中生产这些难以表达的蛋白质的情况,重点是植物系统。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/26ef/8957953/e2340364acd9/fbioe-10-835637-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/26ef/8957953/5975c8c90c49/fbioe-10-835637-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/26ef/8957953/35d862b08878/fbioe-10-835637-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/26ef/8957953/8a3619100e1f/fbioe-10-835637-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/26ef/8957953/e2340364acd9/fbioe-10-835637-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/26ef/8957953/5975c8c90c49/fbioe-10-835637-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/26ef/8957953/35d862b08878/fbioe-10-835637-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/26ef/8957953/8a3619100e1f/fbioe-10-835637-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/26ef/8957953/e2340364acd9/fbioe-10-835637-g004.jpg

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