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.

Development of DNA Nanostructures for High-Affinity Binding to Human Serum Albumin

Abstract: The development of nucleic acid therapeutics has been hampered by issues associated with their stability and in vivo delivery. To address these challenges, we describe a new strategy to engineer DNA structures with strong binding affinity to human serum albumin (HSA). HSA is the most abundant protein in the blood and has a long circulation half-life (19 days). It has been shown to hinder phagocytosis, is retained in tumors, and aids in cellular penetration. Indeed, HSA has already been successfully used for the delivery of small-molecule drugs and nanoparticles. We show that conjugating dendritic alkyl chains to DNA creates amphiphiles that exhibit high-affinity (Kd in low nanomolar range) binding to HSA. Notably, complexation with HSA did not hinder the activity of silencing oligonucleotides inside cells, and the degradation of DNA strands in serum was significantly slowed. We also show that, in a site-specific manner, altering the number and orientation of the amphiphilic ligand on a self-assembled DNA ...

Photo‐conjugation of 8–methoxypsoralen with proteins

Abstract: — 8–Methoxypsoralen (8–MOP) is shown to form a covalent conjugate with bovine serum albumin (BSA) by UVA irradiation in the presence of 02. The photoreaction is shown to involve oxidation of 8–MOP itself as a first step, producing an oxidation product which reacts readily with protein. Thus, this photoreaction appears to be completely different from the known 8–MOP photo-cycloaddition reaction with DNA. Among several proteins studied, human serum albumin, histone type 11, RNAse A and lysozyme also undergo photoinduced addition by 8–MOP. Chemical modifications of various amino acid residues in BSA revealed tyrosine-OH as one of the reaction sites. Irradiation (12 h) with UVA at 1.78 J/ds intensity resulted in approximately 1.5 mot of 8–MOP bound to 1 mol of BSA.

Molecular basis of the Cotton effects induced by the binding of curcumin to human serum albumin

Abstract: Curcumin binding to human serum albumin (HSA) has been found recently to induce bisignate CD curves due to intramolecular exciton coupling between the two feruloyl chromophoric parts The present study reports further results on this interaction UV–vis and chiroptical properties of HSA-bound curcumin were analyzed in detail by comparison with bilirubin–albumin complexes Data obtained by UV–vis and fluorescence spectroscopy, CD displacement experiments and molecular modelling methods suggested the primary binding site of curcumin to be located in site I of HSA Since acid–base dissociation of the polyphenol type curcumin molecule plays a fundamental role in albumin binding, light absorption spectra of curcumin and half-curcumin (dehydrozingerone) were studied in ethanol and in water at different pH values It is established that the phenolic OH group of curcumin is the most acidic and that its dissociation is responsible for both the large red-shift of the main absorption band and the binding of curcumin to HSA in a right-handed chiral conformation Additionally, it is demonstrated that pH dependent induced CD spectra can be utilized to determine the acid–base dissociation constant; from chiroptical data the first pKa value of curcumin was calculated (828)

Secretion of human serum albumin from Bacillus subtilis.

Abstract: We have fused the structural gene (hsa) for human serum albumin (HSA) to the expression elements and signal sequence coding region of each of two genes from Bacillus amyloliquefaciens P, an alpha-amylase gene (amyBamP) and a neutral protease gene (nprBamP). Bacillus subtilis strains harboring either of these gene fusions synthesized a protein with the antigenic characteristics and size (68 kilodaltons) of HSA. Results from pulse-labeling studies indicated that the bacterially produced HSA was secreted from cells which had been converted to protoplasts. Results from similar studies with intact cells suggested that the signal sequence was removed from the hybrid protein, providing further evidence that B. subtilis can translocate this foreign protein across the cell membrane. Signal sequence removal was efficient when the level of HSA synthesis was low. However, in strains which synthesized HSA at a high level, signal sequence removal was less efficient.

Conformational Study of Human Serum Albumin in Pre-denaturation Temperatures by Differential Scanning Calorimetry, Circular Dichroism and UV Spectroscopy

Abstract: Thermal conformational changes of human serum albumin (HSA) in phosphate buffer, 10 mM at pH = 7 are investigated using differential scanning calorimetric (DSC), circular dichroism (CD) and UV spectroscopic methods. The results indicate that temperature increment from 25 degrees C to 55 degrees C induces reversible conformational changes in the structure of HSA. Conformational change of HSA are shown to be a three-step process. Interestingly, melting temperature of the last domain is equal to the maximum value of fever in pathological conditions, i.e. 42 degrees C. These conformational alterations are accompanied by a mild alteration of secondary structures. Study of HSA-SDS (sodium dodecyl sulphate) interaction at 45 degrees C and 35 degrees C reveals that SDS affects the HSA structure at least in three steps: the first two steps result in more stabilization and compactness of HSA structure, while the last one induces the unfolding of HSA. Since HSA has a more affinity for SDS at 45 degrees C compared to 35 degrees C, It is suggested that the net negative charge of HSA is decreased in fever, which results in the decrease of HSA-associated cations and plasma osmolarity, and consequently, heat removal via the increase in urine volume.