Binding studies of aristololactam-β-d-glucoside and daunomycin to human serum albumin

RSC Advances ◽  
2014 ◽  
Vol 4 (62) ◽  
pp. 33082-33090 ◽  
Author(s):  
Abhi Das ◽  
Gopinatha Suresh Kumar
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Studies ◽  
Biophysical Techniques

The binding of two carbohydrate containing molecules aristololactam-β-d-glucoside and daunomycin with human serum albumin was evaluated by biophysical techniques.

Molecular Dynamics Simulation and Binding Studies of β-Sitosterol with Human Serum Albumin and Its Biological Relevance

2010 ◽  
Vol 114 (27) ◽  
pp. 9054-9062 ◽  
Author(s):  
Babu Sudhamalla ◽  
Mahesh Gokara ◽  
Navjeet Ahalawat ◽  
Damu G. Amooru ◽  
Rajagopal Subramanyam
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulation ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Dynamics Simulation ◽  
Binding Studies ◽  
Biological Relevance

scholarly journals Binding Studies of AICAR and Human Serum Albumin by Spectroscopic, Theoretical, and Computational Methodologies

Molecules ◽  
2020 ◽  
Vol 25 (22) ◽  
pp. 5410
Author(s):  
Shokoufeh Hashempour ◽  
Nahid Shahabadi ◽  
Aishat Adewoye ◽  
Brennen Murphy ◽  
Camaray Rouse ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Fluorescence Quenching ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Site ◽  
Conformational Changes ◽  
Flufenamic Acid ◽  
Drug Candidate ◽  
Protein Fluorescence ◽  
Binding Studies

The interactions of small molecule drugs with plasma serum albumin are important because of the influence of such interactions on the pharmacokinetics of these therapeutic agents. 5-Aminoimidazole-4-carboxamide ribonucleoside (AICAR) is one such drug candidate that has recently gained attention for its promising clinical applications as an anti-cancer agent. This study sheds light upon key aspects of AICAR’s pharmacokinetics, which are not well understood. We performed in-depth experimental and computational binding analyses of AICAR with human serum albumin (HSA) under simulated biochemical conditions, using ligand-dependent fluorescence sensitivity of HSA. This allowed us to characterize the strength and modes of binding, mechanism of fluorescence quenching, validation of FRET, and intermolecular interactions for the AICAR–HSA complexes. We determined that AICAR and HSA form two stable low-energy complexes, leading to conformational changes and quenching of protein fluorescence. Stern–Volmer analysis of the fluorescence data also revealed a collision-independent static mechanism for fluorescence quenching upon formation of the AICAR–HSA complex. Ligand-competitive displacement experiments, using known site-specific ligands for HSA’s binding sites (I, II, and III) suggest that AICAR is capable of binding to both HSA site I (warfarin binding site, subdomain IIA) and site II (flufenamic acid binding site, subdomain IIIA). Computational molecular docking experiments corroborated these site-competitive experiments, revealing key hydrogen bonding interactions involved in stabilization of both AICAR–HSA complexes, reaffirming that AICAR binds to both site I and site II.

scholarly journals Enantioresolution and Binding Affinity Studies on Human Serum Albumin: Recent Applications and Trends

Chemosensors ◽  
2021 ◽  
Vol 9 (11) ◽  
pp. 304
Author(s):  
Tony Cardoso ◽  
Ana Sofia Almeida ◽  
Fernando Remião ◽  
Carla Fernandes
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Binding Affinity ◽  
Bioactive Compounds ◽  
High Performance ◽  
Binding Studies ◽  
Chiral Drugs ◽  
Innovative Methods ◽  
Chemistry Research

The interaction between proteins and drugs or other bioactive compounds has been widely explored over the past years. Several methods for analysis of this phenomenon have been developed and improved. Nowadays, increasing attention is paid to innovative methods, such as high performance affinity liquid chromatography (HPALC) and affinity capillary electrophoresis (ACE), taking into account various advantages. Moreover, the development of separation methods for the analysis and resolution of chiral drugs has been an area of ongoing interest in analytical and medicinal chemistry research. In addition to bioaffinity binding studies, both HPALC and ACE al-low one to perform other type of analyses, namely, displacement studies and enantioseparation of racemic or enantiomeric mixtures. Actually, proteins used as chiral selectors in chromatographic and electrophoretic methods have unique enantioselective properties demonstrating suitability for the enantioseparation of a large variety of chiral drugs or other bioactive compounds. This review is mainly focused in chromatographic and electrophoretic methods using human serum albumin (HSA), the most abundant plasma protein, as chiral selector for binding affinity analysis and enantioresolution of drugs. For both analytical purposes, updated examples are presented to highlight recent applications and current trends.

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