Abstract
Crystal formation on air bubble–liquid interface, as soft template to efficiently prompt nucleation of proteins.
Highlights
IntroductionWith the growth of interest in protein drugs in the pharmaceutical industries, the crystallisation of proteins has gradually shifted focus to the manufacture of stable and more controllable products at a larger scale, instead of production of large single crystals for crystallography
The objective of the present study is to investigate the relation between gas-liquid interfaces and protein crystallisation, including the influence on the nucleation and crystal growth
To study the static bubble effect on the protein crystallisation, the traditional hanging droplet was compared to the droplet injected with one air bubble, as shown in Figure 1 (b) and (c), respectively
Summary
With the growth of interest in protein drugs in the pharmaceutical industries, the crystallisation of proteins has gradually shifted focus to the manufacture of stable and more controllable products at a larger scale, instead of production of large single crystals for crystallography. One of the major advantages of protein crystallisation in biopharmaceuticals is the stability of the crystalline structure during drug formulation, storage and delivery [1,2]. These crystallisation processes provide products with higher purities and with potentially lower production costs [3]. MIP and LB nanotemplates can facilitate salt crystallisation in addition to proteins nucleation [14]
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