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Marine Structural Protein Stability Induced by Hofmeister Salt Annealing and Enzymatic Cross-Linking
ACS Biomaterials Science & Engineering ( IF 5.4 ) Pub Date : 2020-08-27 , DOI: 10.1021/acsbiomaterials.0c00791
Anise M. Grant 1 , Michelle C. Krecker 1 , Maneesh K. Gupta 2 , Patrick B. Dennis 2 , Marquise G. Crosby 2 , Vladimir V. Tsukruk 1
Affiliation  

The Humboldt squid is one of the fiercest marine predators thanks in part to its sucker ring teeth that are biopolymer blends of a protein isoform family called suckerin with compression strength that rivals silkworm silk. Here, we focus on the popular suckerin-12 isoform to understand what makes the secondary structure of this biopolymer different in water and the potential role of diverse physical and chemical cross-linkings. By choosing a salt post-treatment, in accordance with the Hofmeister series, we achieved film stability with salt annealing that is comparable to chemical cross-links. By correlating the film morphology with the protein secondary structure changes, suckerin-12 films were shown to contract upon treatment with kosmotropic salts and exhibited increased stability in water. These changes are related to the rearrangement of suckerin-12 secondary structure from random coils and helices to β-sheets. Overall, understanding secondary structure changes caused by aqueous and ionic environments can be instructive for the tuning of the suckerin film sclerotization, its conversion to a tough biological material, and to ultimately produce the natural squid sucker ring teeth.

中文翻译:

Hofmeister盐退火和酶促交联诱导的海洋结构蛋白稳定性

洪堡鱿鱼是最猛烈的海洋捕食者之一,部分原因是它的吸盘齿是由称为吸盘的蛋白质同工型家族的生物聚合物混合物制成的,具有与蚕丝抗衡的抗压强度。在这里,我们集中于流行的suckerin-12同工型,以了解是什么使这种生物聚合物的二级结构在水中与众不同,以及各种物理和化学交联的潜在作用。通过选择盐后处理,根据Hofmeister系列,我们可以通过盐退火获得与化学交联相当的膜稳定性。通过将膜的形态与蛋白质的二级结构变化相关联,可知suckerin-12膜在使用共溶盐处理后会收缩,并在水中表现出更高的稳定性。这些变化与suckerin-12二级结构从无规卷曲和螺旋到β-折叠的重排有关。总体而言,了解由水和离子环境引起的二级结构变化,对于吸盘膜硬化过程的调整,将其转化为坚韧的生物材料以及最终生产出天然的鱿鱼吸盘环齿都具有指导意义。
更新日期:2020-10-12
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