Untitled

Cheruvallath, V.K; Riley, Christopher M.; Narayanan, Sunanda R.; Lindenbaum, Siegfried; Perrin, John H.

doi:10.1023/a:1016066325476

Cited by 28 publications

(9 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…7,58 This triad of residues is highly conserved in mammalian albumins, 59 indicating the importance of intermolecular interactions at this location. However, for FA4 the carboxylate head-groups of fatty acids are hydrogen-bonded to Arg410, Tyr411, and Ser489, which are the most important residues for IBU binding as well.…”

Section: Fa3/fa4 Binding Sitementioning

confidence: 99%

“…Plasmatic fatty acids probably modulate competitively and allosterically IBU binding to HSA, which could explain the experimental dissociation equilibrium constant value of 10 À6 M for the IBU-HSA interaction system. 7,58 This triad of residues is highly conserved in mammalian albumins, 59 indicating the importance of intermolecular interactions at this location.…”

Section: Fa3/fa4 Binding Sitementioning

confidence: 99%

See 1 more Smart Citation

Quantum molecular modelling of ibuprofen bound to human serum albumin

et al. 2015

View full text Add to dashboard Cite

The binding of the nonsteroidal anti-inflammatory drug ibuprofen (IBU) to human serum albumin (HSA) is investigated using density functional theory (DFT) calculations within a fragmentation strategy.Crystallographic data for the IBU-HSA supramolecular complex shows that the ligand is confined to a large cavity at the subdomain IIIA and at the interface between the subdomains IIA and IIB, whose binding sites are FA3/FA4 and FA6, respectively. The interaction energy between the IBU molecule and each amino acid residue of these HSA binding pockets was calculated using the Molecular Fractionation with Conjugate Caps (MFCC) approach employing a dispersion corrected exchange-correlation functional. Our investigation shows that the total interaction energy of IBU bound to HSA at binding sites of the fatty acids FA3/FA4 (FA6) converges only for a pocket radius of at least 8.5Å, mainly due to the action of residues Arg410, Lys414 and Ser489 (Lys351, Ser480 and Leu481) and residues in nonhydrophobic domains, namely Ile388, Phe395, Phe403, Leu407, Leu430, Val433, and Leu453 (Phe206, Ala210, Ala213, and Leu327), which is unusual. Our simulations are valuable for a better understanding of the binding mechanism of IBU to albumin and can lead to the rational design and the development of novel IBU-derived drugs with improved potency.

show abstract

Section: Fa3/fa4 Binding Sitementioning

confidence: 99%

Section: Fa3/fa4 Binding Sitementioning

confidence: 99%

Quantum molecular modelling of ibuprofen bound to human serum albumin

et al. 2015

View full text Add to dashboard Cite

show abstract

“…Several studies have suggested that R-and S-ibuprofen have one common binding site on the HSA [35,44,75]. In addition, S-ibuprofen had at least one other major binding region [35,44,75]. The association equilibrium constant for R-ibuprofen with HSA has been estimated to be 5.3 × 10 5 M −1 at pH 6.9 and 25°C.…”

Section: Chiral Separation Of Racemic Ibuprofenmentioning

confidence: 99%

Development of an affinity silica monolith containing human serum albumin for chiral separations

Mallik

Hage

2008

Journal of Pharmaceutical and Biomedical Analysis

106

View full text Add to dashboard Cite

An affinity monolith based on silica and containing immobilized human serum albumin (HSA) was developed and evaluated in terms of its binding, efficiency and selectivity in chiral separations. The results were compared with data obtained for the same protein when used as a chiral stationary phase with HPLC-grade silica particles or a monolith based on a copolymer of glycidyl methacrylate (GMA) and ethylene dimethacrylate (EDMA). The surface coverage of HSA in the silica monolith was similar to values obtained with silica particles and a GMA/EDMA monolith. However, the higher surface area of the silica monolith gave a material that contained 1.3-2.2-times more immobilized HSA per unit volume when compared to silica particles or a GMA/EDMA monolith. The retention, efficiency and resolving power of the HSA silica monolith were evaluated using two chiral analytes: d/l-tryptophan and R/S-warfarin. The separation of R- and S-ibuprofen was also considered. The HSA silica monolith gave higher retention and higher or comparable resolution and efficiency when compared with HSA columns that contained silica particles or a GMA/EDMA monolith. The silica monolith also gave lower back pressures and separation impedances than these other materials. It was concluded that silica monoliths can be valuable alternatives to silica particles or GMA/EDMA monoliths when used with immobilized HSA as a chiral stationary phase.

show abstract

“…In this article, we propose a chemical model for determining the mutual and specific lowaffinity binding sites. We use HSA as a model protein because it is a major drug carrier protein in blood and has large binding capacity for most drugs and endogenous metabolites [26][27][28][29][30][31]. Two non-steroidal anti-inflammatory drugs, tolmetin (TOL) and salicylic acid (SAL), were used as ligands.…”

Section: Introductionmentioning

confidence: 99%