PRODUCT LITERATURE

Hydration-Induced Structural Changes in the Solid State of Protein:A SAXS/WAXS Study on Lysozyme

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The stability of biologically produced pharmaceuticals is thelimiting factor to various applications, which can be improved by formulationin solid-state forms, mostly via lyophilization. Knowledge about the proteinstructure at the molecular level in the solid state and its transition uponrehydration is however scarce, and yet it most likely affects the physical andchemical stability of the biological drug. In this work, synchrotron small- andwide-angle X-ray scattering (SWAXS) are used to characterize the structureof a model protein, lysozyme, in the solid state and its structural transitionupon rehydration to the liquid state. The results show that the proteinundergoes distortion upon drying to adopt structures that can continuouslyfill the space to remove the protein−air interface that may be formed upondehydration. Above a hydration threshold of 35 wt %, the native structure ofthe protein is recovered. The evolution of SWAXS peaks as a function ofwater content in a broad range of concentrations is discussed in relation tothe structural changes in the protein. Thefindings presented here can be used for the design and optimization of solid-stateformulations of proteins with improved stability.

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: .,

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Language

English

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NONE

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Subject(s)

Inbumin
Solid State Protein

Specific Detail Info

Mol. Pharmaceutics 2020, 17, 9, 3246–3258

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