Fatty acid binding to serum albumin: Molecular simulation approaches
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منابع مشابه
Molecular dynamics simulation and docking studies on the binding properties of several anticancer drugs to human serum albumin
Disposition and transportation of anticancer drugs by human serum albumin (HSA) affects their bioavailability, distribution and elimination. In this study, the interaction of a set of anticancer drugs with HSA was investigated by molecular dynamics and molecular docking simulations. The drugs' activities were analyzed according to their docking scores, binding sites and structural descriptors. ...
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متن کاملFatty acid binding to plasma albumin.
A review of the available information about fatty acid binding to plasma albumin is presented. Albumin is composed of a single polypeptide chain, folded so as to form three or four spherical units. The strong fatty acid binding sites probably are located in crevices between these spherical regions. The anionic form of the fatty acid binds to albumin. Most of the binding energy comes from nonpol...
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Human serum albumin (HSA) is an important protein that carries variety of substances like some hormones and drugs in blood. Pharmacological studies of the interaction of many drugs and HSA are reported during several decades, specially recently years. Interaction of cortisol and fluoxetine hydrochloride (FLX) (as a common anti-stress drug) with HSA (as their carrier in blood) has been studied s...
متن کاملFluoxetin Competes with Cortisol for Binding to Human Serum Albumin
Human serum albumin (HSA) is an important protein that carries variety of substances like some hormones and drugs in blood. Pharmacological studies of the interaction of many drugs and HSA are reported during several decades, specially recently years. Interaction of cortisol and fluoxetine hydrochloride (FLX) (as a common anti-stress drug) with HSA (as their carrier in blood) has been studied s...
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - General Subjects
سال: 2013
ISSN: 0304-4165
DOI: 10.1016/j.bbagen.2013.03.032