Interaction studies unveil potential binding sites on bovine serum albumin for gut metabolite trimethylamine n-oxide (TMAO)
Abstract Trimethylamine-N-oxide (TMAO) is gut microbiota-derived metabolite, plays a critical role in human health and diseases such as metabolic, cardiovascular, colorectal cancer and, neurological disorders. Binding interactions between TMAO and serum albumins are crucial to understand the impact...
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BMC
2025-01-01
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| Series: | BMC Chemistry |
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| Online Access: | https://doi.org/10.1186/s13065-024-01375-0 |
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| author | Awadhesh Kumar Verma Payal Gulati GBVS Lakshmi Anand Mohan Neeta Raj Sharma Pratima R. Solanki Anil Kumar |
| author_facet | Awadhesh Kumar Verma Payal Gulati GBVS Lakshmi Anand Mohan Neeta Raj Sharma Pratima R. Solanki Anil Kumar |
| author_sort | Awadhesh Kumar Verma |
| collection | DOAJ |
| description | Abstract Trimethylamine-N-oxide (TMAO) is gut microbiota-derived metabolite, plays a critical role in human health and diseases such as metabolic, cardiovascular, colorectal cancer and, neurological disorders. Binding interactions between TMAO and serum albumins are crucial to understand the impact of TMAO on disease mechanisms. However, detailed insights into the interaction mechanisms, preferred binding locations, and conformational changes in BSA upon binding TMAO are still unclear. TMAO interacts with serum albumin in human body and thus, a model study of interaction for TMAO-BSA conjugate is presented in support of it. Decrease in absorbance intensity of protein upon interaction with metabolites reveals conjugate formation, while fluorescence spectroscopy indicate static quenching. Contact angle measurements further reveal the hydrophilic nature of the TMAO-BSA complex, while CD and FTIR support conformational changes in BSA upon binding but structure remain intact. Computational studies, such as molecular docking, molecular dynamics simulation and, MM/GBSA, confirm a stable complex with a binding energy of − 3.6 kcal/mol. These findings provide a foundation for understanding the pharmacodynamics and pharmacokinetics of TMAO and may aid in developing strategies for treating diseases, such as chronic kidney disease and neurological disorder where TMAO-serum albumins interaction are implicated. |
| format | Article |
| id | doaj-art-48f92f3cd7714d13af948306e3ae62b2 |
| institution | Kabale University |
| issn | 2661-801X |
| language | English |
| publishDate | 2025-01-01 |
| publisher | BMC |
| record_format | Article |
| series | BMC Chemistry |
| spelling | doaj-art-48f92f3cd7714d13af948306e3ae62b22025-01-26T12:13:09ZengBMCBMC Chemistry2661-801X2025-01-0119111510.1186/s13065-024-01375-0Interaction studies unveil potential binding sites on bovine serum albumin for gut metabolite trimethylamine n-oxide (TMAO)Awadhesh Kumar Verma0Payal Gulati1GBVS Lakshmi2Anand Mohan3Neeta Raj Sharma4Pratima R. Solanki5Anil Kumar6Special Centre for Nanoscience, Jawaharlal Nehru UniversityGene Regulation Laboratory, National Institute of ImmunologySpecial Centre for Nanoscience, Jawaharlal Nehru UniversitySchool of Bioengineering and Biosciences, Lovely Professional UniversitySchool of Bioengineering and Biosciences, Lovely Professional UniversitySpecial Centre for Nanoscience, Jawaharlal Nehru UniversityGene Regulation Laboratory, National Institute of ImmunologyAbstract Trimethylamine-N-oxide (TMAO) is gut microbiota-derived metabolite, plays a critical role in human health and diseases such as metabolic, cardiovascular, colorectal cancer and, neurological disorders. Binding interactions between TMAO and serum albumins are crucial to understand the impact of TMAO on disease mechanisms. However, detailed insights into the interaction mechanisms, preferred binding locations, and conformational changes in BSA upon binding TMAO are still unclear. TMAO interacts with serum albumin in human body and thus, a model study of interaction for TMAO-BSA conjugate is presented in support of it. Decrease in absorbance intensity of protein upon interaction with metabolites reveals conjugate formation, while fluorescence spectroscopy indicate static quenching. Contact angle measurements further reveal the hydrophilic nature of the TMAO-BSA complex, while CD and FTIR support conformational changes in BSA upon binding but structure remain intact. Computational studies, such as molecular docking, molecular dynamics simulation and, MM/GBSA, confirm a stable complex with a binding energy of − 3.6 kcal/mol. These findings provide a foundation for understanding the pharmacodynamics and pharmacokinetics of TMAO and may aid in developing strategies for treating diseases, such as chronic kidney disease and neurological disorder where TMAO-serum albumins interaction are implicated.https://doi.org/10.1186/s13065-024-01375-0TMAOBovine serum albumin (BSA)In silicoDFTDockingSpectroscopy |
| spellingShingle | Awadhesh Kumar Verma Payal Gulati GBVS Lakshmi Anand Mohan Neeta Raj Sharma Pratima R. Solanki Anil Kumar Interaction studies unveil potential binding sites on bovine serum albumin for gut metabolite trimethylamine n-oxide (TMAO) BMC Chemistry TMAO Bovine serum albumin (BSA) In silico DFT Docking Spectroscopy |
| title | Interaction studies unveil potential binding sites on bovine serum albumin for gut metabolite trimethylamine n-oxide (TMAO) |
| title_full | Interaction studies unveil potential binding sites on bovine serum albumin for gut metabolite trimethylamine n-oxide (TMAO) |
| title_fullStr | Interaction studies unveil potential binding sites on bovine serum albumin for gut metabolite trimethylamine n-oxide (TMAO) |
| title_full_unstemmed | Interaction studies unveil potential binding sites on bovine serum albumin for gut metabolite trimethylamine n-oxide (TMAO) |
| title_short | Interaction studies unveil potential binding sites on bovine serum albumin for gut metabolite trimethylamine n-oxide (TMAO) |
| title_sort | interaction studies unveil potential binding sites on bovine serum albumin for gut metabolite trimethylamine n oxide tmao |
| topic | TMAO Bovine serum albumin (BSA) In silico DFT Docking Spectroscopy |
| url | https://doi.org/10.1186/s13065-024-01375-0 |
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