Molecular mechanism of Thioflavin-T binding to amyloid fibrils.

Human serum albumin: from bench to bedside.

Serum albumin first appeared in early vertebrates and is present in the plasma of all mammals. Its canonical structure supported by a conserved set of disulfide bridges is maintained in all mammalian serum albumins and any changes in sequence are highly correlated with evolution of the species. Previous structural investigations of mammalian serum albumins have only concentrated on human serum albumin (HSA), most likely as a consequence of crystallization and diffraction difficulties. Here, the crystal structures of serum albumins isolated from bovine, equine and leporine blood plasma are reported. The structure of bovine serum albumin (BSA) was determined at 2.47 A resolution, two crystal structures of equine serum albumin (ESA) were determined at resolutions of 2.32 and 2.04 A, and that of leporine serum albumin (LSA) was determined at 2.27 A resolution. These structures were compared in detail with the structure of HSA. The ligand-binding pockets in BSA, ESA and LSA revealed different amino-acid compositions and conformations in comparison to HSA in some cases; however, much more significant differences were observed on the surface of the molecules. BSA, which is one of the most extensively utilized proteins in laboratory practice and is used as an HSA substitute in many experiments, exhibits only 75.8% identity compared with HSA. The higher resolution crystal structure of ESA highlights the binding properties of this protein because it includes several bound compounds from the crystallization solution that provide additional structural information about potential ligand-binding pockets.

Structures of bovine, equine and leporine serum albumin.

A comprehensive review on flavanones, the major citrus polyphenols

Ligand binding strategies of human serum albumin: how can the cargo be utilized?

Human serum albumin (HSA), being the most abundant carrier protein in blood and a modern day clinical tool for drug delivery, attracts high attention among biologists. Hence, its unfolding/refolding strategies and exogenous/endogenous ligand binding preference are of immense use in therapeutics and clinical biochemistry. Among its fellow proteins albumin is known to carry almost every small molecule. Thus, it is a potential contender for being a molecular cargo/or nanovehicle for clinical, biophysical and industrial purposes. Nonetheless, its structure and function are largely regulated by various chemical and physical factors to accommodate HSA to its func- tional purpose. This multifunctional protein also possesses enzymatic properties which may be used to convert prodrugs to active therapeutics. This review aims to highlight current overview on the binding strategies of protein to various ligands that may be expected to lead to significant clinical applications. Chirality 00:000-000, 2009. V C 2009 Wiley-Liss, Inc.

Review Article Ligand Binding Strategies of Human Serum Albumin: How Can the Cargo be Utilized?

Interactions of thioflavin T with serum albumins: spectroscopic analyses.

The interactions among bovine, rabbit, and porcine serum albumins and single-chain cationic surfactant cetyltrimethylammonium bromide (CTAB) versus its gemini counterpart (designated as G4) have be...

Priyankar Sen

Papers

Ligand binding strategies of human serum albumin: how can the cargo be utilized?

Review Article Ligand Binding Strategies of Human Serum Albumin: How Can the Cargo be Utilized?

Interactions of thioflavin T with serum albumins: spectroscopic analyses.

Interaction of bovine (BSA), rabbit (RSA), and porcine (PSA) serum albumins with cationic single-chain/gemini surfactants: a comparative study.

Spectroscopic studies on the interaction of cationic surfactants with bovine serum albumin.