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Enhanced Stabilization in Dried Silk Fibroin Matrices
Biomacromolecules ( IF 6.2 ) Pub Date : 2017-08-23 00:00:00 , DOI: 10.1021/acs.biomac.7b00857
Adrian B. Li , Jonathan A. Kluge , Miaochan Zhi 1 , Marcus T. Cicerone 1 , Fiorenzo G. Omenetto , David L. Kaplan
Affiliation  

Preliminary studies have shown that silk fibroin can protect biomacromolecules from thermal degradation, but a deeper understanding of underlying mechanisms needed to fully leverage the stabilizing potential of this matrix has not been realized. In this study, we investigate stabilization of plasma C-reactive protein (CRP), a diagnostic indicator of infection or inflammation, to gain insight into stabilizing mechanisms of silk. We observed that the addition of antiplasticizing excipients that suppress β-relaxation amplitudes in silk matrices resulted in enhanced stability of plasma CRP. These observations are consistent with those made in sugar-glass-based protein-stabilizing matrices and suggest fundamental insight into mechanisms as well as practical strategies to employ with silk protein matrices for enhanced stabilization utility.

中文翻译:

干燥丝素蛋白基质的增强稳定性

初步研究表明,丝素蛋白可以保护生物大分子免受热降解,但尚未充分了解充分利用该基质稳定潜力所需的潜在机制。在这项研究中,我们调查了血浆C反应蛋白(CRP)的稳定性(一种感染或炎症的诊断指标),以深入了解丝绸的稳定机制。我们观察到,抑制丝基质中β松弛幅度的抗增塑赋形剂的添加可增强血浆CRP的稳定性。这些观察结果与在基于糖玻璃的蛋白质稳定化基质中获得的观察结果一致,并暗示了对与丝绸蛋白质基质结合使用以增强稳定化效用的机制以及实用策略的基本见解。
更新日期:2017-08-23
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