کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
5372703 1504185 2017 9 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Interactions of human serum albumin with doxorubicin in different media
ترجمه فارسی عنوان
تعامل آلبومین سرم انسان با دوکسوروبیسین در رسانه های مختلف
موضوعات مرتبط
مهندسی و علوم پایه شیمی شیمی تئوریک و عملی
چکیده انگلیسی


- Doxorubicin interactions with human serum albumin analyzed by 1H NMR spectroscopy and cryoporometry.
- Doxorubicin cations displace a fraction of water bound to HSA molecules.
- Water shell of HSA molecules is very non-uniform and affected by bound doxorubicin.

Interactions of human serum albumin (10 wt% H2O and 0.3 wt% sodium caprylate) with doxorubicin hydrochloride (1 wt%) were studied alone or with addition of HCl (3.6 wt% HCl) using 1H NMR spectroscopy. A model of hydrated HSA/12DOX was calculated using PM7 method with COSMO showing large variations in the binding constant depending on structural features of DOX/HSA complexes. DOX molecules/ions displace bound water from narrow intramolecular voids in HSA that leads to diminution of freezing-melting point depression of strongly bound water (SBW). Structure of weakly bound water (WBW) depends much weaker on the presence of DOX than SBW because a major fraction of DOX is bound to adsorption sites of HSA. Addition of HCl results in strong changes in structure of macromolecules and organization of water in hydration shells of HSA (i.e., mainly SBW) and in the solution (i.e., WBW + non-bound bulk water).

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ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Chemical Physics - Volumes 483–484, 1 February 2017, Pages 26-34
نویسندگان
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