Journals / ACADEMIC PLATFORM-JOURNAL OF ENGINEERING AND SCIENCE / 2020 / Cilt: 8 - Sayı: 3

Physical Insights into the Bio-preservation of Proteins by Glassy Solvents: Why is Glycerol better than Trehalose at low Temperatures?

Pages
580–584
DOI
—
🏛️Bibliographic metadata and full text access for this article are provided via DergiPark.
DergiPark Record ↗
✨

AI Summary & Key Takeaways

AI Insight
⚡ TL;DR(Too Long; Didn't Read)

We traced the basis of this phenomenon to the different temperature dependencies of the intermolecular hydrogen bonds between the model protein structure and the surrounding solvent.

📌 3 Key Takeaways

🎯
Objective & Hypothesis:Biopreservation has been a critical area of technical and scientific research as it enables various forms of biomolecular therapeutic agents to find practical use in medicine.
📊
Key Findings & Data:The mechanism at which biomimicry-inspired solutions to stabilize biomolecules has been of great scientific interest.
💡
Conclusion & Impact:We traced the basis of this phenomenon to the different temperature dependencies of the intermolecular hydrogen bonds between the model protein structure and the surrounding solvent.
🔬Design:Modeling & Simulation
📍Scope:Comprehensive Sample
⚙️Variables:Domain Parameters

Özet

Biopreservation has been a critical area of technical and scientific research as it enables various forms of biomolecular therapeutic agents to find practical use in medicine. The mechanism at which biomimicry-inspired solutions to stabilize biomolecules has been of great scientific interest. We have studied the behavior of lysozyme immersed in glycerol and trehalose, two solvents frequently used in the bio-preservation of proteins, with the purpose of identifying the microscopic origins of their very different dynamical suppression capabilities. In agreement with experiments, we find that glycerol is superior to trehalose at low temperatures, although the latter is deeper in the glassy state, while trehalose is better at higher temperatures. We traced the basis of this phenomenon to the different temperature dependencies of the intermolecular hydrogen bonds between the model protein structure and the surrounding solvent.

🔖

Cite This Article

DİRAMA, T. E. (2020). Physical Insights into the Bio-preservation of Proteins by Glassy Solvents: Why is Glycerol better than Trehalose at low Temperatures?. ACADEMIC PLATFORM-JOURNAL OF ENGINEERING AND SCIENCE, Cilt: 8 - Sayı: 3, 580–584. https://ajindex.com/articles/354896

📄 Full Text PDF Viewer

📄

PDF görüntüleyici hazırlanıyor...

References (1)

  1. . M. Tollinger, K. A. Crowhurst, L. E. Kay, and J. D. Forman-Kay, “Site-specific contributions to the pH dependence of protein stability,” Proc. Natl. Acad. Sci., vol. 100, no. 8, pp. 4545–4550, 2003. [2]. T. J. Magliery and L. Regan, “Combinatorial approaches to protein stability and structure,” Eur. J. Biochem., vol. 271, no. 9, pp. 1595–1608, 2004. [3]. P. H. Yancey, “Organic osmolytes as compatible, metabolic and counteracting cytoprotectants in high osmolarity and other stresses,” J. Exp. Biol., vol. 208, no. 15, pp. 2819–2830, 2005. [4]. Mei Yang-woytowitz, Charles Yu, and Timothy Wiles, “Kits for the detection of beta-lactamases,” 8389234. [5]. V. R. Garigapati, D. Su, R. Khanzada, and S. J. Sawamura, “Protein stabilization formulations,” US8435943B2, 2013. [6]. Ali Eroglu, “Compositions and Methods for Biopreservation,” US20190098891A1, 2018. [7]. H. Faghihi, S. Merrikhihaghi, A. Ruholamini Najafabadi, V. Ramezani, S. Sardari, and A. Vatanara, “A Comparative Study to Evaluate the Effect of Different Carbohydrates on the Stability of Immunoglobulin G during Lyophilization and Following Storage,” Pharm. Sci., vol. 22, no. 4, pp. 251–259, 2016. [8]. K. Gekko and S. N. Timasheff, “Mechanism of protein stabilization by glycerol: preferential hydration in glycerolwater mixtures,” Biochemistry, vol. 20, no. 16, pp. 4667– 4676, 1981. [9]. M. Uritani, M. Takai, and K. Yoshinaga, “Protective effect of disaccharides on restriction endonucleases during drying under vacuum1,” J. Biochem. (Tokyo), vol. 117, no. 4, pp. 774–779, 1995. [10]. R. B. Gregory, Ed., Protein-solvent interactions. New York, N.Y: M. Dekker, 1995. [11]. G. M. Sastry and N. Agmon, “Trehalose prevents myoglobin collapse and preserves its internal mobility,” Biochemistry, vol. 36, no. 23, pp. 7097–7108, 1997. [12]. A. Ansari et al., “Protein states and proteinquakes.,” Proc. Natl. Acad. Sci., vol. 82, no. 15, pp. 5000–5004, 1985. [13]. G. Caliskan et al., “Protein and solvent dynamics: How strongly are they coupled?,” J. Chem. Phys., vol. 121, no. 4, pp. 1978–1983, 2004. [14]. T. E. Dirama, G. A. Carri, and A. P. Sokolov, “Coupling between lysozyme and glycerol dynamics: Microscopic insights from molecular-dynamics simulations,” J. Chem. Phys., vol. 122, no. 24, p. 244910, 2005. [15]. T. E. Dirama, J. E. Curtis, G. A. Carri, and A. P. Sokolov, “Coupling between lysozyme and trehalose dynamics: Microscopic insights from molecular-dynamics simulations,” J. Chem. Phys., vol. 124, no. 3, p. 034