Kinetic and thermodynamic studies of sunitinib malate interaction with albumin using surface plasmon resonance and molecular docking methods
Kinetic and thermodynamic studies of sunitinib malate interaction with albumin using surface plasmon resonance and molecular docking methods
نویسندگان: سعیده محمدزاده اصل , ایوب آقانژاد , جعفر عزتی نژاد دولت آبادی
کلمات کلیدی: Sunitinib malate; SPR; Molecular docking; Kinetic; Thermodynamic; BSA.
نشریه: 24084 , 11 , 150 , 2019
| نویسنده ثبت کننده مقاله |
جعفر عزتی نژاد دولت آبادی |
| مرحله جاری مقاله |
تایید نهایی |
| دانشکده/مرکز مربوطه |
مرکز تحقیقات کاربردی دارویی |
| کد مقاله |
67981 |
| عنوان فارسی مقاله |
Kinetic and thermodynamic studies of sunitinib malate interaction with albumin using surface plasmon resonance and molecular docking methods |
| عنوان لاتین مقاله |
Kinetic and thermodynamic studies of sunitinib malate interaction with albumin using surface plasmon resonance and molecular docking methods |
| ناشر |
5 |
| آیا مقاله از طرح تحقیقاتی و یا منتورشیپ استخراج شده است؟ |
خیر |
| عنوان نشریه (خارج از لیست فوق) |
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| نوع مقاله |
Original Article |
| نحوه ایندکس شدن مقاله |
ایندکس شده سطح یک – ISI - Web of Science |
| آدرس لینک مقاله/ همایش در شبکه اینترنت |
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| Effective transportation of drugs in human body plays a crucial role in treatment procedure. Bovine serum albumin (BSA) is one of the most important drug carriers in mammalian blood circulation system and has a significant role in transportation and delivery of drugs. Anti-cancer drugs such as Sunitinib malate can bind and be transported by means of BSA. Therefore, evaluation of BSA interaction with Sunitinib malate is necessary because it influences drug temperament such as lifetime and its activity. Poor bindings result in weak drug distribution, whereas strong interaction of BSA with Sunitinib malate leads to lesser amount of free drug in plasma. The interaction between BSA and Sunitinib malate was done by surface plasmon resonance (SPR) method. Kinetic and thermodynamic parameters were calculated for BSA interaction with Sunitinib malate. Kinetic parameters showed that the affinity of BSA to Sunitinib malate was decreased as temperature was increased. Also, estimation of thermodynamic parameters represented positive values for enthalpy and entropy, which indicated that BSA binds to Sunitinib malate through hydrophobic force. Finally, molecular docking study was done in order to find out the Sunitinib malate interaction site at BSA. Molecular docking analysis showed that lowest binding energy belongs to site IIIB indicating more affinity of this subdomain for drug. |
| نام فایل |
تاریخ درج فایل |
اندازه فایل |
دانلود |
| Kinetic and thermodynamic studies of sunitinib malate interaction with albumin using surface plasmon resonance and molecular docking methods.pdf | 1398/04/27 | 1537064 | دانلود |