Topic
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.
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TL;DR: The binding constants and free energy corresponding to experimental and computational analysis suggest that there are hydrophobic and hydrophilic interactions when piperine binds to HSA and AGP and prove that the HSA–piperine complex is stable in nature.
Abstract: Human serum albumin (HSA) and α-1-acid glycoprotein (AGP) (acute phase protein) are the plasma proteins in blood system which transports many drugs. To understand the pharmacological importance of ...
72 citations
TL;DR: P pH-profiles showed that the interaction between IS and DNSA was very sensitive to the N to B transition: “competitive-like” strong allosteric regulation was observed for binding of the two ligands to theN conformer, whereas in the B conformation binding of these molecules was nearly “independent”.
Abstract: Purpose. The study was performed for clarifying the mechanism of interaction between indoxyl sulfate (IS), a typical uremic toxin bound to site II, and site I-ligands when bound to human serum albumin (HSA). The effect of the N to B transition on the interactions was also examined.
72 citations
TL;DR: Current insights into the effects of FA binding on HSA are reviewed, focusing on the biophysical insights obtained using molecular simulation approaches such as docking, molecular dynamics (MD), and binding free energy calculations.
71 citations
TL;DR: Three large fragments of human serum albumin produced by peptic digestion of the native protein show similar circular-dichroism spectra to that of the complex between bilirubin and whole albumin, in agreement with affinity-labeling work on albumin with reactive ligands where substitution occurs in the N-terminal region of the molecule.
Abstract: Three large fragments of human serum albumin were produced by peptic digestion of the native protein [Geisow & Beaven (1977) Biochem. J. 161, 619-625]. Fragment P44 represents residues 1-386 and fragments P29 and P31 represent residues 49-307 and residues 308-584 respectively of the albumin molecule. The large N-terminal fragment P44 has a similar percentage of alpha-helix to stored defatted albumin, although the alpha-helix content of all the fragments is significantly less than that of freshly prepared albumin. The fragment P44 appears to account for all the binding of the hydrophobic probe 8-anilinonaphthalene-1-sulphonate to albumin. N-Acetyl-L-tryptophan binds to this fragment and displaces one of the bound molecules of 8-anilinonaphthalene-1-sulphonate. Bilirubin binds to fragments P44 and P29, and the complexes show similar circular-dichroism spectra to that of the complex between bilirubin and whole albumin. These results are in agreement with affinity-labeling work on albumin with reactive ligands where substitution occurs in the N-terminal region of the molecule. The sharp conformational transitional transition in albumin which is observed between pH4 and 3.5 was absent from the fragments. This isomerization, usually called the N-F transition, probably occurs in intact albumin as a result of the unfolding or separation of the C-terminal third of the protein from the remainder of the molecule.
71 citations
TL;DR: A system in which proteins can be photochemically patterned in three dimensions within hydrogels under physiological conditions and allows protein immobilization under mild conditions and can be broadly applied to any protein expressed as an ABD fusion.
71 citations