Effects of disulfide bridges and backbone connectivity on water sorption by protein matrices
Abstract Understanding the water sorption behavior of protein powders is important in applications such as the preservation of protein-based pharmaceuticals. Most globular proteins exhibit a characteristic sigmoidal water adsorption isotherm at ambient conditions. However, it is not well understood...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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Nature Portfolio
2017-08-01
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| Series: | Scientific Reports |
| Online Access: | https://doi.org/10.1038/s41598-017-08561-2 |
| _version_ | 1818749450704650240 |
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| author | Sang Beom Kim Rakesh S. Singh Prem K. C. Paul Pablo G. Debenedetti |
| author_facet | Sang Beom Kim Rakesh S. Singh Prem K. C. Paul Pablo G. Debenedetti |
| author_sort | Sang Beom Kim |
| collection | DOAJ |
| description | Abstract Understanding the water sorption behavior of protein powders is important in applications such as the preservation of protein-based pharmaceuticals. Most globular proteins exhibit a characteristic sigmoidal water adsorption isotherm at ambient conditions. However, it is not well understood how water sorption behavior is influenced by intrinsic factors that are related to structural properties of proteins. We investigate computationally how structural constraints on proteins influence the water sorption isotherms of amorphous protein powders. Specifically, we study the effects of non-local disulfide linkages and backbone connectivity using pheromone ER-23 and lysozyme as model proteins. We find that non-local disulfide linkages can significantly restrict structural changes during hydration and dehydration, and this in turn greatly reduces the extent of hysteresis between the adsorption and desorption branches. Upon removing the backbone connectivity by breaking all peptide bonds in lysozyme, we find that the hysteresis shifts towards the lower humidity regime, and the water uptake capacity is significantly enhanced. We attribute these changes to the higher aggregation propensity of the constraint-free amino acids in dehydrated condition, and the formation of a spanning water network at high hydration levels. |
| first_indexed | 2024-12-18T04:03:59Z |
| format | Article |
| id | doaj.art-3515ff3e8ea345ea908c4aac632319cf |
| institution | Directory Open Access Journal |
| issn | 2045-2322 |
| language | English |
| last_indexed | 2024-12-18T04:03:59Z |
| publishDate | 2017-08-01 |
| publisher | Nature Portfolio |
| record_format | Article |
| series | Scientific Reports |
| spelling | doaj.art-3515ff3e8ea345ea908c4aac632319cf2022-12-21T21:21:38ZengNature PortfolioScientific Reports2045-23222017-08-01711910.1038/s41598-017-08561-2Effects of disulfide bridges and backbone connectivity on water sorption by protein matricesSang Beom Kim0Rakesh S. Singh1Prem K. C. Paul2Pablo G. Debenedetti3Department of Chemical and Biological Engineering, Princeton UniversityDepartment of Chemical and Biological Engineering, Princeton UniversityUnilever R&D, Port Sunlight LaboratoryDepartment of Chemical and Biological Engineering, Princeton UniversityAbstract Understanding the water sorption behavior of protein powders is important in applications such as the preservation of protein-based pharmaceuticals. Most globular proteins exhibit a characteristic sigmoidal water adsorption isotherm at ambient conditions. However, it is not well understood how water sorption behavior is influenced by intrinsic factors that are related to structural properties of proteins. We investigate computationally how structural constraints on proteins influence the water sorption isotherms of amorphous protein powders. Specifically, we study the effects of non-local disulfide linkages and backbone connectivity using pheromone ER-23 and lysozyme as model proteins. We find that non-local disulfide linkages can significantly restrict structural changes during hydration and dehydration, and this in turn greatly reduces the extent of hysteresis between the adsorption and desorption branches. Upon removing the backbone connectivity by breaking all peptide bonds in lysozyme, we find that the hysteresis shifts towards the lower humidity regime, and the water uptake capacity is significantly enhanced. We attribute these changes to the higher aggregation propensity of the constraint-free amino acids in dehydrated condition, and the formation of a spanning water network at high hydration levels.https://doi.org/10.1038/s41598-017-08561-2 |
| spellingShingle | Sang Beom Kim Rakesh S. Singh Prem K. C. Paul Pablo G. Debenedetti Effects of disulfide bridges and backbone connectivity on water sorption by protein matrices Scientific Reports |
| title | Effects of disulfide bridges and backbone connectivity on water sorption by protein matrices |
| title_full | Effects of disulfide bridges and backbone connectivity on water sorption by protein matrices |
| title_fullStr | Effects of disulfide bridges and backbone connectivity on water sorption by protein matrices |
| title_full_unstemmed | Effects of disulfide bridges and backbone connectivity on water sorption by protein matrices |
| title_short | Effects of disulfide bridges and backbone connectivity on water sorption by protein matrices |
| title_sort | effects of disulfide bridges and backbone connectivity on water sorption by protein matrices |
| url | https://doi.org/10.1038/s41598-017-08561-2 |
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