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

Abstract

Biopreservation has been a critical area of technical and scientific research as it enables various forms biomolecular therapeutic agents to find practical use in medicine. The mechanism at which biomimicry-inspired solutions to stabilize biomolecules has been of a 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 and the surrounding solvent.

Keywords

• structural dynamics
• protein
• solvent
• biopreservation

Proteinlerin Camsı Solventlerle Biyolojik Korunması Üzerine Fiziksel Bilgiler: Gliserol, Düşük Sıcaklıklarda Neden Trehaloz'dan Daha İyidir?

Abstract

Biyokoruma, çeşitli formlarda biyomoleküler terapötik ajanların tıpta pratik kullanım bulmasını sağlayan kritik bir teknik ve bilimsel araştırma alanı olmuştur. Temelini biyomimikriden alan biyomolekülleri stabilize eden çözümlerin çalışma prensipleri bilimsel ilgi odağı olmuştur. Bu çalışmada, lizozimin proteinlerin biyolojik olarak korunmasında sıkça kullanılan iki çözücü olan gliserol ve trehaloz içerisindeki davranışlarını, bu çözücülerin birbirinden farklı olan dinamik bastırma yeteneklerinin mikroskobik kökenlerini belirlemek amacıyla inceledik. Gliserolün düşük sıcaklıklarda trehaloza (trehalozun daha derin bir camsı halde olmasına rağmen) üstün olduğunu, trehalozun ise yüksek sıcaklıklarda daha etkin olduğunu gözlemledik. Bu sonucun kökeninin protein ve çözücü arasındaki moleküller arası hidrojen bağlarının farklı sıcaklık bağımlılıklarına sahip oldukları sonucuna vardık.

Keywords

• yapısal dinamik
• protein
• çözücü
• biyokoruma

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