scispace - formally typeset
Search or ask a question
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.


Papers
More filters
Journal ArticleDOI
25 Mar 2009-Langmuir
TL;DR: The results support that strong binding occurs at the hydrophobic moieties of HSA and fibrinogen, excluding water access, and lead to effective suppression of degradation of curcumin.
Abstract: The use of curcumin as an effective wound healing agent is of significant interest currently. It is well established that curcumin undergoes rapid degradation in physiological buffer by hydrolysis. The means by which curcumin is stabilized at the wound site to enable healing is poorly understood because blood plasma is composed of approximately 92% water. Plasma proteins, which constitute the remaining 6-8%, has been shown to stabilize curcumin. It is, however, still unclear which proteins are responsible for this phenomenon. In this study, the effects of major plasma proteins, which include human serum albumin (HSA), fibrinogen, immunoglobulin G (IgG), and transferrin, on stabilizing curcumin are investigated. In particular, we investigate their effects on the hydrolysis of curcumin at pH 7.4. In the presence of both transferrin and IgG, curcumin continues to undergo rapid hydrolysis but this reaction is suppressed by the presence of either HSA or fibrinogen with an impressive yield of approximately 95%. Furthermore, the binding constants of curcumin to HSA and fibrinogen are on the order of 10(4) and 10(5) M(-1), respectively. The binding constants of transferrin and IgG, however, are at least 1 order of magnitude less than those of HSA and fibrinogen. The results support that strong binding occurs at the hydrophobic moieties of HSA and fibrinogen, excluding water access. Therefore, strong interactions with HSA and fibrinogen inhibit hydrolysis of curcumin and in turn lead to effective suppression of degradation.

179 citations

Journal ArticleDOI
TL;DR: HSA structure was less perturbed by polyamine analogues compared to those of the biogenic polyamines, and the protein secondary structure showed major alterations, indicating partial protein unfolding upon polyamine interaction.

178 citations

Journal ArticleDOI
TL;DR: The protein binding of diazepam, indomethacin, salicylic acid, sulfadimetoxine and warfarin in serum of uremic patients has been studied by equilibrium dialysis and circular dichroism measurements and compared with that in normal serum.

177 citations

Journal ArticleDOI
TL;DR: HSA conformation was stabilized by cholesterol and DOPE with a slight increase of protein alpha-helical structures, while DOTAP and DDAB induced an important (alpha-->beta) transition, suggesting a partial protein unfolding.
Abstract: Human serum albumin (HSA) is a major transporter for delivering several endogenous compounds including fatty acids in vivo. Even though HSA is the primary target of fatty acid binding, the effects of cationic lipid on protein stability and conformation have not been investigated. The aim of this study was to examine the interaction of human serum albumin (HSA) with helper lipids--cholesterol (Chol) and dioleoylphosphatidylethanolamine (DOPE)--and with cationic lipids--dioctadecyldimethylammonium bromide (DDAB) and 1,2-dioleoyl-3-trimethylammonium-propane (DOTAP), at physiological conditions, using constant protein concentration and various lipid contents. Fourier transform infrared (FTIR), circular dichroism (CD), and fluorescence spectroscopic methods were used to analyze the lipid binding mode, the binding constant, and the effects of lipid interaction on HSA stability and conformation. Structural analysis showed that cholesterol and DOPE (helper lipids) interact mainly with HSA polypeptide polar groups and via hydrophobic moieties. Hydrophobic interactions dominate the binding of cationic lipids to HSA. The number of bound lipids (n) calculated was 1.22 (cholesterol), 1.82 (DDAB), 1.76 (DOPE), and 1.56 (DOTAP). The overall binding constants estimated were KChol=2.3 (+/-0.50)x10(3) M(-1), KDDAB=8.9 (+/-0.95)x10(3) M(-1), KDOTAP=9.1 (+/-0.90)x10(3) M(-1), and KDOPE=4.7 (+/-0.70)x10(3) M(-1). HSA conformation was stabilized by cholesterol and DOPE with a slight increase of protein alpha-helical structures, while DOTAP and DDAB induced an important (alpha-->beta) transition, suggesting a partial protein unfolding.

177 citations


Network Information
Related Topics (5)
In vivo
61.3K papers, 1.9M citations
84% related
Amino acid
124.9K papers, 4M citations
83% related
Aqueous solution
189.5K papers, 3.4M citations
82% related
Glutathione
42.5K papers, 1.8M citations
82% related
Cell culture
133.3K papers, 5.3M citations
80% related
Performance
Metrics
No. of papers in the topic in previous years
YearPapers
2023174
2022423
2021284
2020333
2019333
2018337