Denaturation studies on bovine serum albumin–bile salt system: Bile salt stabilizes bovine serum albumin through hydrophobicity
Protein denaturation is under intensive research, since it leads to neurological disorders of severe consequences. Avoiding denaturation and stabilizing the proteins in their native state is of great importance, especially when proteins are used as drug molecules or vaccines. It is preferred to add...
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| Format: | Article |
| Language: | English |
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Elsevier
2018-02-01
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| Series: | Journal of Pharmaceutical Analysis |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2095177917300734 |
| _version_ | 1819295653390450688 |
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| author | Karpagaraj Malarkani Ivy Sarkar Susithra Selvam |
| author_facet | Karpagaraj Malarkani Ivy Sarkar Susithra Selvam |
| author_sort | Karpagaraj Malarkani |
| collection | DOAJ |
| description | Protein denaturation is under intensive research, since it leads to neurological disorders of severe consequences. Avoiding denaturation and stabilizing the proteins in their native state is of great importance, especially when proteins are used as drug molecules or vaccines. It is preferred to add pharmaceutical excipients in protein formulations to avoid denaturation and thereby stabilize them. The present study aimed at using bile salts (BSs), a group of well-known drug delivery systems, for stabilization of proteins. Bovine serum albumin (BSA) was taken as the model protein, whose association with two BSs, namely sodium cholate (NaC) and sodium deoxycholate (NaDC), was studied. Denaturation studies on the pre-formed BSA-BS systems were carried out under chemical and physical denaturation conditions. Urea was used as the chemical denaturant and BSA-BS systems were subjected to various temperature conditions to understand the thermal (physical) denaturation. With the denaturation conditions prescribed here, the data obtained is informative on the association of BSA-BS systems to be hydrophobic and this effect of hydrophobicity plays an important role in stabilizing the serum albumin in its native state under both chemical and thermal denaturation. |
| first_indexed | 2024-12-24T04:45:38Z |
| format | Article |
| id | doaj.art-2e648019a1dd48f8afc1c379b2797b09 |
| institution | Directory Open Access Journal |
| issn | 2095-1779 |
| language | English |
| last_indexed | 2024-12-24T04:45:38Z |
| publishDate | 2018-02-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Journal of Pharmaceutical Analysis |
| spelling | doaj.art-2e648019a1dd48f8afc1c379b2797b092022-12-21T17:14:41ZengElsevierJournal of Pharmaceutical Analysis2095-17792018-02-0181273610.1016/j.jpha.2017.06.007Denaturation studies on bovine serum albumin–bile salt system: Bile salt stabilizes bovine serum albumin through hydrophobicityKarpagaraj Malarkani0Ivy Sarkar1Susithra Selvam2Department of Chemistry, Vel Tech University, Avadi, Chennai 600062, IndiaDepartment of Chemistry, Indian Institute of Technology Madras, Chennai 600036, IndiaDepartment of Chemistry, Vel Tech University, Avadi, Chennai 600062, IndiaProtein denaturation is under intensive research, since it leads to neurological disorders of severe consequences. Avoiding denaturation and stabilizing the proteins in their native state is of great importance, especially when proteins are used as drug molecules or vaccines. It is preferred to add pharmaceutical excipients in protein formulations to avoid denaturation and thereby stabilize them. The present study aimed at using bile salts (BSs), a group of well-known drug delivery systems, for stabilization of proteins. Bovine serum albumin (BSA) was taken as the model protein, whose association with two BSs, namely sodium cholate (NaC) and sodium deoxycholate (NaDC), was studied. Denaturation studies on the pre-formed BSA-BS systems were carried out under chemical and physical denaturation conditions. Urea was used as the chemical denaturant and BSA-BS systems were subjected to various temperature conditions to understand the thermal (physical) denaturation. With the denaturation conditions prescribed here, the data obtained is informative on the association of BSA-BS systems to be hydrophobic and this effect of hydrophobicity plays an important role in stabilizing the serum albumin in its native state under both chemical and thermal denaturation.http://www.sciencedirect.com/science/article/pii/S2095177917300734Bile saltsBovine serum albuminChemical denaturationThermal denaturationTryptophan fluorescenceProtein stabilization |
| spellingShingle | Karpagaraj Malarkani Ivy Sarkar Susithra Selvam Denaturation studies on bovine serum albumin–bile salt system: Bile salt stabilizes bovine serum albumin through hydrophobicity Journal of Pharmaceutical Analysis Bile salts Bovine serum albumin Chemical denaturation Thermal denaturation Tryptophan fluorescence Protein stabilization |
| title | Denaturation studies on bovine serum albumin–bile salt system: Bile salt stabilizes bovine serum albumin through hydrophobicity |
| title_full | Denaturation studies on bovine serum albumin–bile salt system: Bile salt stabilizes bovine serum albumin through hydrophobicity |
| title_fullStr | Denaturation studies on bovine serum albumin–bile salt system: Bile salt stabilizes bovine serum albumin through hydrophobicity |
| title_full_unstemmed | Denaturation studies on bovine serum albumin–bile salt system: Bile salt stabilizes bovine serum albumin through hydrophobicity |
| title_short | Denaturation studies on bovine serum albumin–bile salt system: Bile salt stabilizes bovine serum albumin through hydrophobicity |
| title_sort | denaturation studies on bovine serum albumin bile salt system bile salt stabilizes bovine serum albumin through hydrophobicity |
| topic | Bile salts Bovine serum albumin Chemical denaturation Thermal denaturation Tryptophan fluorescence Protein stabilization |
| url | http://www.sciencedirect.com/science/article/pii/S2095177917300734 |
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