Carbohydrate-Based Macromolecular Crowding-Induced Stabilization of Proteins: Towards Understanding the Significance of the Size of the Crowder
There are a large number of biomolecules that are accountable for the extremely crowded intracellular environment, which is totally different from the dilute solutions, i.e., the idealized conditions. Such crowded environment due to the presence of macromolecules of different sizes, shapes, and comp...
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| Format: | Article |
| Language: | English |
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MDPI AG
2019-09-01
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| Series: | Biomolecules |
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| Online Access: | https://www.mdpi.com/2218-273X/9/9/477 |
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| author | Sumra Shahid Ikramul Hasan Faizan Ahmad Md. Imtaiyaz Hassan Asimul Islam |
| author_facet | Sumra Shahid Ikramul Hasan Faizan Ahmad Md. Imtaiyaz Hassan Asimul Islam |
| author_sort | Sumra Shahid |
| collection | DOAJ |
| description | There are a large number of biomolecules that are accountable for the extremely crowded intracellular environment, which is totally different from the dilute solutions, i.e., the idealized conditions. Such crowded environment due to the presence of macromolecules of different sizes, shapes, and composition governs the level of crowding inside a cell. Thus, we investigated the effect of different sizes and shapes of crowders (ficoll 70, dextran 70, and dextran 40), which are polysaccharide in nature, on the thermodynamic stability, structure, and functional activity of two model proteins using UV-Vis spectroscopy and circular dichroism techniques. We observed that (a) the extent of stabilization of α-lactalbumin and lysozyme increases with the increasing concentration of the crowding agents due to the excluded volume effect and the small-sized and rod-shaped crowder, i.e., dextran 40 resulted in greater stabilization of both proteins than dextran 70 and ficoll 70; (b) structure of both the proteins remains unperturbed; and (c) enzymatic activity of lysozyme decreases with the increasing concentration of the crowder. |
| first_indexed | 2024-12-22T20:01:59Z |
| format | Article |
| id | doaj.art-226903ea8e1d47369754172b3507a100 |
| institution | Directory Open Access Journal |
| issn | 2218-273X |
| language | English |
| last_indexed | 2024-12-22T20:01:59Z |
| publishDate | 2019-09-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Biomolecules |
| spelling | doaj.art-226903ea8e1d47369754172b3507a1002022-12-21T18:14:15ZengMDPI AGBiomolecules2218-273X2019-09-019947710.3390/biom9090477biom9090477Carbohydrate-Based Macromolecular Crowding-Induced Stabilization of Proteins: Towards Understanding the Significance of the Size of the CrowderSumra Shahid0Ikramul Hasan1Faizan Ahmad2Md. Imtaiyaz Hassan3Asimul Islam4Centre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, Jamia Nagar, New Delhi 110025, IndiaDepartment of Basic Medical Science, Faculty of applied Medical Sciences, Al-Baha University, PO Box: 1988- Al-Baha 65411, Saudi ArabiaCentre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, Jamia Nagar, New Delhi 110025, IndiaCentre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, Jamia Nagar, New Delhi 110025, IndiaCentre for Interdisciplinary Research in Basic Sciences, Jamia Millia Islamia, Jamia Nagar, New Delhi 110025, IndiaThere are a large number of biomolecules that are accountable for the extremely crowded intracellular environment, which is totally different from the dilute solutions, i.e., the idealized conditions. Such crowded environment due to the presence of macromolecules of different sizes, shapes, and composition governs the level of crowding inside a cell. Thus, we investigated the effect of different sizes and shapes of crowders (ficoll 70, dextran 70, and dextran 40), which are polysaccharide in nature, on the thermodynamic stability, structure, and functional activity of two model proteins using UV-Vis spectroscopy and circular dichroism techniques. We observed that (a) the extent of stabilization of α-lactalbumin and lysozyme increases with the increasing concentration of the crowding agents due to the excluded volume effect and the small-sized and rod-shaped crowder, i.e., dextran 40 resulted in greater stabilization of both proteins than dextran 70 and ficoll 70; (b) structure of both the proteins remains unperturbed; and (c) enzymatic activity of lysozyme decreases with the increasing concentration of the crowder.https://www.mdpi.com/2218-273X/9/9/477carbohydrate-based macromolecular crowderprotein foldingthermodynamic stabilitycrowder sizeexcluded volume |
| spellingShingle | Sumra Shahid Ikramul Hasan Faizan Ahmad Md. Imtaiyaz Hassan Asimul Islam Carbohydrate-Based Macromolecular Crowding-Induced Stabilization of Proteins: Towards Understanding the Significance of the Size of the Crowder Biomolecules carbohydrate-based macromolecular crowder protein folding thermodynamic stability crowder size excluded volume |
| title | Carbohydrate-Based Macromolecular Crowding-Induced Stabilization of Proteins: Towards Understanding the Significance of the Size of the Crowder |
| title_full | Carbohydrate-Based Macromolecular Crowding-Induced Stabilization of Proteins: Towards Understanding the Significance of the Size of the Crowder |
| title_fullStr | Carbohydrate-Based Macromolecular Crowding-Induced Stabilization of Proteins: Towards Understanding the Significance of the Size of the Crowder |
| title_full_unstemmed | Carbohydrate-Based Macromolecular Crowding-Induced Stabilization of Proteins: Towards Understanding the Significance of the Size of the Crowder |
| title_short | Carbohydrate-Based Macromolecular Crowding-Induced Stabilization of Proteins: Towards Understanding the Significance of the Size of the Crowder |
| title_sort | carbohydrate based macromolecular crowding induced stabilization of proteins towards understanding the significance of the size of the crowder |
| topic | carbohydrate-based macromolecular crowder protein folding thermodynamic stability crowder size excluded volume |
| url | https://www.mdpi.com/2218-273X/9/9/477 |
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