Bile salts-bovine serum albumin binding: spectroscopic and thermodynamic studies

Picó, Guillermo; Houssier, Claude

doi:10.1016/0167-4838(89)90209-4

Cited by 21 publications

(9 citation statements)

References 11 publications

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“…In the presence of NaChol-Ala, the Trp214 experienced a more hydrophobic region, which may be attributed to the presence of hydrophobic Chol moieties. In fact, the binding of bile salts to HSA and BSA are also known to occur through hydrophobic interactions. , This means NaChol-Ala binds to hydrophobic pocket of HSA near Trp214. To be sure of it, we further performed DLS measurements with the protein (0.1%) in the absence and presence of NaChol-Ala.…”

Section: Results and Discussionmentioning

confidence: 99%

Spontaneously Formed Robust Steroidal Vesicles: Physicochemical Characterization and Interaction with HSA

2014

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Self-assembled multimolecular aggregates, such as vesicles, have earned tremendous attention for their applications as model membranes and drug delivery systems. Over the past decades, enormous efforts have been dedicated to the development of stable and biocompatible vesicles that form spontaneously in aqueous solution. With the aim of preparing highly stable vesicles, we herein report the physicochemical characterization of a novel cholesterol-based chiral surfactant with l-alanine headgroup. Different techniques, such as surface tensiometry, fluorescence spectroscopy, dynamic light scattering, UV-vis spectroscopy, transmission electron microscopy, and confocal fluorescence microscopy were employed to investigate the self-assembly properties of the aforementioned single-tailed steroidal surfactant in aqueous solution. The surfactant molecule is weakly surface-active, but self-assembles to form unilamellar vesicles facilitated by the strong hydrophobic association of the cholesterol moieties, above a very low critical aggregation concentration. The vesicles are fairly stable with respect to aging, temperature, and pH of the aqueous medium. Additionally, the vesicles were found to fuse together, leading to large unilamellar vesicles. The intervesicular fusion pertaining to high stability of the vesicles could be ascribed to large hydrophobic interactions among steroidal skeletons. Furthermore, the interaction of the vesicles with human serum albumin is also investigated.

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Section: Results and Discussionmentioning

confidence: 99%

Spontaneously Formed Robust Steroidal Vesicles: Physicochemical Characterization and Interaction with HSA

2014

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“…All bile acids are albumin bound. The albumin-bile acid interaction is by "back-toback" association, which means that the hydrophobic face of the bile acid molecule interacts with the hydrophobic groups of albumin via Van der Waals forces (Pico and Houssier 1989). The hydroxyl groups are essential for such interaction since they render the molecules amphiphatic.…”

Section: Structure Activity Relationship In Hepatobiliary Clearance Omentioning

confidence: 99%

“…The hydroxyl groups are essential for such interaction since they render the molecules amphiphatic. For instance, a model compound without such hydroxyl groups, 5~-cholanic acid, is associated with albumin only by electrostatic forces due to its carboxyl group (Pico and Houssier 1989). The heart-shaped structure of human serum albumin contains several subdomains with binding sites for ligands in subdomains IIA and IIIA (He and Carter 1992).…”

Section: Structure Activity Relationship In Hepatobiliary Clearance Omentioning

confidence: 99%

Transport of organic anions in the liver. An update on bile acid, fatty acid, monocarboxylate, anionic amino acid, cholephilic organic anion, and anionic drug transport

Petzinger¹

1994

Reviews of Physiology, Biochemistry and Pharmacology

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“…15 The polar substitutions (number, position, and type) on the steroid ring significantly govern the binding affinity of bile salts with proteins. 16 Human serum albumin, HSA, a transport protein, consists of 585 amino acid residues and is characterized by a low tryptophan (Trp) and high cysteine content, stabilizing a series of nine loops. 17 The secondary structure of native HSA is composed of ∼67% α-helix with six turns and 17 disulfide bridges, and the tertiary structure of HSA is composed of three domains, I−III, each of which is further subdivided into two subdomains, A and B.…”

Section: Introductionmentioning

confidence: 99%

“…Bile salts form reversible complexes with serum proteins, which play an important role in the transport of these ligands from the blood to the liver . The polar substitutions (number, position, and type) on the steroid ring significantly govern the binding affinity of bile salts with proteins …”

Section: Introductionmentioning

confidence: 99%

Hydrophobicity Is the Governing Factor in the Interaction of Human Serum Albumin with Bile Salts

2015

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The present study demonstrates a detailed characterization of the interaction of a series of bile salts, sodium deoxycholate (NaDC), sodium cholate (NaC), and sodium taurocholate (NaTC), with a model transport protein, human serum albumin (HSA). Here, steady-state and time-resolved fluorescence spectroscopic techniques have been used to characterize the interaction of the bile salts with HSA. The binding isotherms constructed from steady-state fluorescence intensity measurements demonstrate that the interaction of the bile salts with HSA can be characterized by three distinct regions, which were also successfully reproduced from the significant variation of the emission wavelength (λ(em)) of the intrinsic tryptophan (Trp) moiety of HSA. The time-resolved fluorescence decay behavior of the Trp residue of HSA was also found to corroborate the steady-state results. The effect of interaction with the bile salts on the native conformation of the protein has been explored in a circular dichroism (CD) study, which reveals a decrease in α-helicity of HSA induced by the bile salts. In accordance with this, the esterase activity of the protein-bile salt aggregates is found to be reduced in comparison to that of the native protein. Our results exclusively highlight the fact that it is the hydrophobic character of the bile salt that governs the extent of interaction with the protein. Isothermal titration calorimetry (ITC) and molecular docking studies further substantiate our other experimental findings.

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Bile salts-bovine serum albumin binding: spectroscopic and thermodynamic studies

Cited by 21 publications

References 11 publications

Spontaneously Formed Robust Steroidal Vesicles: Physicochemical Characterization and Interaction with HSA

Spontaneously Formed Robust Steroidal Vesicles: Physicochemical Characterization and Interaction with HSA

Transport of organic anions in the liver. An update on bile acid, fatty acid, monocarboxylate, anionic amino acid, cholephilic organic anion, and anionic drug transport

Hydrophobicity Is the Governing Factor in the Interaction of Human Serum Albumin with Bile Salts

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