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: Present data indicate a novel role of fatty acids as allosteric inhibitors of flavonoid bioavailability, and appear to be relevant in rationalizing the interference between dietary compounds, food supplements, and drugs.
116 citations
TL;DR: The receptor specific interactions of GNR-BBN conjugates provide realistic opportunities in the design and development of in vivo molecular imaging and therapy agents for cancer.
Abstract: Gastrin releasing protein receptor specific bombesin (BBN) peptide-gold nanoconjugates were successfully synthesized using gold nanorods and dithiolated peptide. The gold nanorod-bombesin (GNR-BBN) conjugates showed extraordinary in vitro stabilities against various biomolecules including NaCl, cysteine, histidine, bovine serum albumin, human serum albumin, and dithiothreitol. Quantitative measurements on the binding affinity (IC(50)) of GNR-BBN conjugates toward prostate and breast tumor cells were evaluated. The IC(50) values establish that GNR-BBN conjugates have strong affinity toward the gastrin releasing peptide receptors on both the tumors. Detailed cellular interaction studies of GNR-BBN conjugates revealed that nanorods internalize via a receptor-mediated endocytosis pathway. The receptor specific interactions of GNR-BBN conjugates provide realistic opportunities in the design and development of in vivo molecular imaging and therapy agents for cancer.
116 citations
TL;DR: It is concluded that ITCC-labeled Tf and HSA can serve as macromolecular contrast agents for the optical imaging of tumors, with Tf-ITCC showing higher efficiency.
Abstract: Macromolecules accumulate in solid tumors and can thus be used as carriers for the delivery of attached contrast agents to tumors. We report the synthesis and use of serum protein–dye conjugates consisting of transferrin (Tf) or human serum albumin (HSA) and an indotricarbocyanine (ITCC) derivative as contrast agents for the optical imaging of tumors. The compounds were characterized with respect to their photophysical properties and tested in vitro for their ability to bind to tumor cells and in vivo for their potential to delineate experimental tumors. In contrast to HAS-ITTC, Tf-ITCC showed receptor-mediated uptake by HT29 human colon cancer cells in vitro. After intravenous injection into HT29 tumor-bearing nude mice both compounds induced increased fluorescence contrast of tumors in vivo. After 24 h the contrast between tumor and normal tissue was significantly higher for Tf-ITCC than for HAS-ITCC. Dye-induced fluorescence was found to be predominantly located in perinecrotic areas of the tumor. Furthermore, Tf-ITCC produced fluorescence of viable tumor cells, whereas HAS-ITCC fluorescence was recorded along connective tissue. We conclude that ITCC-labeled Tf and HSA can serve as macromolecular contrast agents for the optical imaging of tumors, with Tf-ITCC showing higher efficiency.
116 citations
TL;DR: The protein conformation was altered with major reduction of α-helix from 60 to 55% to 40 to 40% and increase of β-structure from 22 to 15% (free HSA) to 33 to 23% in the drug- Protein secondary, structure are attributed to partial, unfolding of HSA on drug complexation.
Abstract: We report different analytical methods used to study the effects of 3′-azido-3′-deoxythymidine, aspirin, taxol, cisplatin, atrazine, 2,4-dichlorophenoxyacetic, biogenic, polyamines, chlorophyll, chlorophyllin, poly(ethylene glycol), vanadyl cation, vanadate anion, cobalt-hexamine cation, and As2O3, on the stability and secondary structure of human serum albumin (HSA) in aqueous solution, using capillary electrophoresis. Fourier transform infrared, ultraviolet visible, and circular dichroism (CD) spectroscopic methods. The concentrations of HSA used were 4% to 2% or 0.6 to 0.3 mM, while different ligand concentrations were 1μM to 1 mM. Structural data showed drugs are mostly located along the polypeptide chains with both specific and nonspecific interactions. The stability of drug-protein complexes were in the order KVO2+ 1.2×108M−1>KAZT 1.9×106M−1>KPEG 4.1×105M−1>Katrazine 3.5×104M−1>Kchlorophyll 2.9×104M−1>K2,4-D2.5×104 M−1>Kspermine 1.7×104M−1>Ktaxol 1.43×104M−1>KCo3+>1.1×104M−1>Kaspirin 1.04×104i−1>Kchlorophyllin 7.0×103M−1×KVO3−6.0×103M−1>Kspermidine 5.4 ×103M−1>Kputrescine 3.9×103M−1>KAs2O3, 2.2×103M−1>Kcisplatin 1.2×102M−1. The protein conformation was altered (infrared and CD results) with major reduction of α-helix from 60 to 55% (free HSA) to 40 to 40% and increase of β-structure from 22 to 15% (free HSA) to 33 to 23% in the drug-protein complexes. The alterations of protein secondary, structure are attributed to partial, unfolding of HSA on drug complexation.
116 citations
TL;DR: Both experimental results and modeling methods suggested that AQ binds mainly to the sub-domain IIA of HSA, and the efficiency of energy transfer and distance between HSA and acceptor AQ was calculated.
116 citations