Topic
Human serum albumin
About: Human serum albumin is a research topic. Over the lifetime, 9402 publications have been published within this topic receiving 269029 citations. The topic is also known as: serum albumin & ALB.
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TL;DR: The impressively high imprinting factor reached, exceeding 20, strongly confirmed that semi-covalent imprinting resulted in formation of a large number of very well defined molecular cavities with high affinity to the HSA molecules.
118 citations
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TL;DR: The present work reveals a protein conformation change upon P5W30 binding, a new feature not explicitly documented in previous studies, which is a simple exothermic process, with several binding sites.
Abstract: The molecular recognition of polyoxometalates by human serum albumin is studied using two different polyoxometalates (POMs) at pH 7.5. The results are compared with those obtained at pH 3.5 and 9.0. At pH 7.5, both POMs strongly interact with the protein with different binding behaviors. The Keggin shaped POM, [H2W12O40]6- (H2W12), specifically binds the protein, forming a complex with a 1:1 stoichiometry with Ka = 2.9 × 106 M-1. The binding constant decreased dramatically with the increase of the ionic strength, thus indicating a mostly electrostatic binding process. Isothermal titration calorimetry (ITC) experiments show that the binding is an enthalpically driven exothermic process. For the wheel shaped POM [NaP5W30O110]14- (P5W30), there are up to five binding sites on the protein. Increasing the ionic strength changes the binding behavior significantly, leading to a simple exothermic process, with several binding sites. Competitive binding experiments indicate that the two POMs share one common bindi...
118 citations
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TL;DR: Compound 9a could effectively intercalate into Calf Thymus DNA to form 9a-DNA complex which might block DNA replication to exert their powerful antimicrobial activities, thus improving its antimicrobial efficacy.
118 citations
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TL;DR: The effects of albumin on the geometry of human erythrocytes have been studied as discussed by the authors, where individual red cells, hanging on edge from coverslips, were photographed and digitized using a Gradicon digitizer.
118 citations
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TL;DR: The combined results provide that HA binds to HSA and thus its elimination is hindered and an increase in and is observed from DSC results that indicate increase in stability of HSA upon binding to HA.
Abstract: Binding of hippuric acid (HA), a uremic toxin, with human serum albumin (HSA) has been examined by isothermal titration calorimetry (ITC), differential scanning calorimetry (DSC), molecular docking, circular dichroism (CD) and fluorescence spectroscopy to understand the reason that govern its impaired elimination through hemodialysis. ITC results shows that the HA binds with HSA at high (Kb ∼104) and low affinity (Kb ∼103) sites whereas spectroscopic results predict binding at a single site (Kb∼103). The HA form complex with HSA that involves electrostatic, hydrogen and hydrophobic binding forces as illustrated by calculated thermodynamic parameters. Molecular docking and displacement studies collectively revealed that HA bound to both site I and site II; however, relatively strongly to the later. Esterase-like activity of HSA confirms the involvement of Arg410 and Tyr411 of Sudlow site II in binding of HA. CD results show slight conformational changes occurs in the protein upon ligation that may be responsible for the discrepancy in van’t Hoff and calorimetric enthalpy change. Furthermore, an increase in and is observed from DSC results that indicate increase in stability of HSA upon binding to HA. The combined results provide that HA binds to HSA and thus its elimination is hindered.
118 citations