Binding process evaluation of bovine serum albumin and Lawsonia inermis (henna) through spectroscopic and molecular docking approaches

Binding process evaluation of bovine serum albumin and Lawsonia inermis (henna) through spectroscopic and molecular docking approaches


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صفحه نخست سامانه
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نویسندگان: فاطمه جواهری قزل دیزج , منصور محمودپور , مسعود مقدس زاده , رضا یکتا , جعفر عزتی نژاد دولت آبادی

کلمات کلیدی: Lawsonia inermis Bovine serum albumin Spectroscopic technique Docking simulation

نشریه: 18106 , 115792 , 331 , 2021

اطلاعات کلی مقاله
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نویسنده ثبت کننده مقاله جعفر عزتی نژاد دولت آبادی
مرحله جاری مقاله تایید نهایی
دانشکده/مرکز مربوطه مرکز تحقیقات کاربردی دارویی
کد مقاله 77073
عنوان فارسی مقاله Binding process evaluation of bovine serum albumin and Lawsonia inermis (henna) through spectroscopic and molecular docking approaches
عنوان لاتین مقاله Binding process evaluation of bovine serum albumin and Lawsonia inermis (henna) through spectroscopic and molecular docking approaches
ناشر 6
آیا مقاله از طرح تحقیقاتی و یا منتورشیپ استخراج شده است؟ بلی
عنوان نشریه (خارج از لیست فوق)
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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Lawsonia inermis L. (Henna) has been widely used in cosmetic, medicine and pharmacy industries. Henna is one of the ancient used plants and it can be absorbed into the blood and interact with plasma serum albumin. In this article, we investigated the interaction between henna and bovine serum albumin (BSA) through several spectroscopic techniques, which accompanied with molecular docking approach. According to the results, fluorescence intensity of BSA were decreased upon addition of different concentrations of henna and variation of the intensity illustrates the interaction between henna and BSA. Stern-Volmer quenching analysis along with bimolecular quenching rate results suggested that henna quenched the intensity of BSA through hybrid quenching mechanism, which was con firmed via UV–Vis measurement. As the temperature increase, values of binding constant increased from 5.17 × 102 to 6.17× 102 (M −1) demonstrating that the stability of henna –BSA complex increased with temperature rising. Thermodynamic investigations revealed that the henna molecule bind to BSA via hydrophobic bonds spontaneously. Furthermore, the molecular docking analysis demonstrated that henna has high affinity to bind a cavity in Site II (Domain III, subdomain IIIA) on BSA with binding energy score - 11.37 kcal/mol. Finally, it should be stated that distribution of the henna in the blood circulatory system can be done via BSA, which would accompany us to understand the different medicinal aspects of this natural product especially in drug delivery.

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نویسنده نفر چندم مقاله
فاطمه جواهری قزل دیزجاول
منصور محمودپورسوم
مسعود مقدس زادهچهارم
رضا یکتاپنجم
جعفر عزتی نژاد دولت آبادیششم

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نام فایل تاریخ درج فایل اندازه فایل دانلود
2021.pdf1400/07/251075404دانلود