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Hydration-Induced S...
Hydration-Induced Structural Changes in the Solid State of Protein : A SAXS/WAXS Study on Lysozyme
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- Phan-Xuan, Tuan (författare)
- Malmö University,Malmö universitet,Institutionen för biomedicinsk vetenskap (BMV),Biofilms Research Center for Biointerfaces,Max IV Laboratory, Lund University, 224 84 Lund, Sweden
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- Bogdanova, Ekaterina (författare)
- Malmö University,Malmö universitet,Institutionen för biomedicinsk vetenskap (BMV),Biofilms Research Center for Biointerfaces
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- Millqvist-Fureby, Anna (författare)
- RISE,Kemiska processer och läkemedel,RISE Research Institutes of Sweden, 114 86 Stockholm, Sweden
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- Fransson, Jonas (författare)
- SOBI Swedish Orphan Biovitrum, 112 76 Stockholm, Sweden
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- Terry, Ann E. (författare)
- Lund University,Lunds universitet,MAX IV-laboratoriet,MAX IV Laboratory
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- Kocherbitov, Vitaly (författare)
- Malmö University,Malmö universitet,Institutionen för biomedicinsk vetenskap (BMV),Biofilms Research Center for Biointerfaces
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(creator_code:org_t)
- 2020-08-05
- 2020
- Engelska.
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Ingår i: Molecular Pharmaceutics. - : American Chemical Society. - 1543-8384 .- 1543-8392. ; 17:9, s. 3246-3258
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Abstract
Ämnesord
Stäng
- The stability of biol. produced pharmaceuticals is the limiting factor to various applications, which can be improved by formulation in solid-state forms, mostly via lyophilization. Knowledge about the protein structure at the mol. level in the solid state and its transition upon rehydration is however scarce, and yet it most likely affects the phys. and chem. stability of the biol. drug. In this work, synchrotron small- and wide-angle X-ray scattering (SWAXS) are used to characterize the structure of a model protein, lysozyme, in the solid state and its structural transition upon rehydration to the liquid state. The results show that the protein undergoes distortion upon drying to adopt structures that can continuously fill the space to remove the protein-air interface that may be formed upon dehydration. Above a hydration threshold of 35 wt %, the native structure of the protein is recovered. The evolution of SWAXS peaks as a function of water content in a broad range of concentrations is discussed in relation to the structural changes in the protein. The findings presented here can be used for the design and optimization of solid-state formulations of proteins with improved stability.
Ämnesord
- NATURVETENSKAP -- Biologi -- Biokemi och molekylärbiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Biochemistry and Molecular Biology (hsv//eng)
Nyckelord
- biotherapeutics
- dehydration
- distorted structure
- hydration
- small- and wide-angle X-ray scattering
- solid-state protein
- biotherapeutics
- dehydration
- distorted structure
- hydration
- small- and wide-angle X-ray scattering
- solid-state protein
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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