scholarly journals A Comparative Interaction between Copper Ions with Alzheimer'sβAmyloid Peptide and Human Serum Albumin

2012 ◽  
Vol 2012 ◽  
pp. 1-4 ◽  
Author(s):  
G. Rezaei Behbehani ◽  
L. Barzegar ◽  
M. Mohebbian ◽  
A. A. Saboury
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Copper Ions ◽  
Copper Ion ◽  
Titration Calorimetry ◽  
Solvation Model ◽  
Solvation Parameters ◽  
Induced Aggregation

The interaction of Cu2+with the first 16 residues of the Alzheimer's amyliodβpeptide,Aβ(1–16), and human serum albumin (HSA) were studied in vitro by isothermal titration calorimetry at pH 7.2 and 310 K in aqueous solution. The solvation parameters recovered from the extended solvation model indicate that HSA is involved in the transport of copper ion. Complexes betweenAβ(1–16) and copper ions have been proposed to be an aberrant interaction in the development of Alzheimer's disease, where Cu2+is involved inAβ(1–16) aggregation. The indexes of stability indicate that HSA removed Cu2+fromAβ(1–16), rapidly, decreased Cu-induced aggregation ofAβ(1–16), and reduced the toxicity ofAβ(1–16) + Cu2+significantly.

Nof2206Probing the interaction of memantine, an important Alzheimer's drug, with human serum albumin: In silico and In vitro approach

2021 ◽  
pp. 116888
Author(s):  
Fahad A. Alhumaydhi ◽  
Mohammad Abdullah Aljasir ◽  
Abdullah S.M. Aljohani ◽  
Suliman A. Alsagaby ◽  
Ameen S.S. Alwashmi ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
In Silico

scholarly journals Synthesis and In Vitro Assessment of pH-Sensitive Human Serum Albumin Conjugates of Pirarubicin

2020 ◽  
Vol 14 (1) ◽  
pp. 22
Author(s):  
Kenji Tsukigawa ◽  
Shuhei Imoto ◽  
Keishi Yamasaki ◽  
Koji Nishi ◽  
Toshihiko Tsutsumi ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Coupling Reaction ◽  
Synthetic Polymer ◽  
Ph Sensitive ◽  
Acidic Ph ◽  
Polymer Conjugate ◽  
Acidic Conditions

In a previous study, we reported on the development of a synthetic polymer conjugate of pirarubicin (THP) that was formed via an acid-labile hydrazone bond between the polymer and the THP. However, the synthetic polymer itself was non-biodegradable, which could lead to unexpected adverse effects. Human serum albumin (HSA), which has a high biocompatibility and good biodegradability, is also a potent carrier for delivering antitumor drugs. The objective of this study was to develop pH-sensitive HSA conjugates of THP (HSA-THP), and investigate the release of THP and the cytotoxicity under acidic conditions in vitro for further clinical development. HSA-THP was synthesized by conjugating maleimide hydrazone derivatives of THP with poly-thiolated HSA using 2-iminothiolane, via a thiol-maleimide coupling reaction. We synthesized two types of HSA-THP that contained different amounts of THP (HSA-THP2 and HSA-THP4). Free THP was released from both of the HSA conjugates more rapidly at an acidic pH, and the rates of release for HSA-THP2 and HSA-THP4 were similar. Moreover, both HSA-THPs exhibited a higher cytotoxicity at acidic pH than at neutral pH, which is consistent with the effective liberation of free THP under acidic conditions. These findings suggest that these types of HSA-THPs are promising candidates for further development.

The in Vitro Anti-HIV Efficacy of Negatively Charged Human Serum Albumin Is Antagonized by Heparin

1997 ◽  
Vol 13 (8) ◽  
pp. 677-683 ◽  
Author(s):  
P.J. SWART ◽  
C.S. SUN ◽  
M.E. KUIPERS ◽  
C. ASUNCION ◽  
S. JOSEPHS ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Anti Hiv

scholarly journals Kinetic study of the photochemical changes of (ZZ)-bilirubin IX α bound to human serum albumin. Demonstration of (EZ)-bilirubin IX α as an intermediate in photochemical changes from (ZZ)-bilirubin IX α to (EZ)-cyclobilirubin IX α

1985 ◽  
Vol 226 (1) ◽  
pp. 251-258 ◽  
Author(s):  
S Itoh ◽  
S Onishi
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Kinetic Study ◽  
Human Serum ◽  
Photochemical Reaction ◽  
Relative Rate ◽  
Significant Preference ◽  
Geometrical Isomers ◽  
Relative Rate Constants

The present study was performed to elucidate why the photochemical reaction of (ZZ)-bilirubin bound to human serum albumin is singularly selective, and only one of the two (EZ)- and (ZE)-bilirubins, the (ZE)-isomer, is produced. In a kinetic study of the photochemical reaction in vitro, the sum of the relative rate constants of photochemical transformation of (EZ)-bilirubin into both (EZ)-cyclobilirubin and (ZZ)-bilirubin, with a significant preference for the former, was proved to be considerably larger than that of the transformation of (ZZ)-bilirubin into (EZ)-bilirubin. Therefore only one of the geometrical isomers, namely (ZE)-bilirubin, is apparently formed. It was concluded that (EZ)-bilirubin photochemically undergoes (EZ)-cyclization, i.e. structural photoisomerization, while bound to its high-affinity site on human serum albumin, and is an intermediate in the transformation of (ZZ)-bilirubin into (EZ)-cyclobilirubin.

In vitro studies on the interaction between human serum albumin and fosfomycin disodium salt, an antibiotic drug by multi-spectroscopic and molecular docking methods

2014 ◽  
Vol 41 (4) ◽  
pp. 2377-2387 ◽  
Author(s):  
Manjunath D. Meti ◽  
Kirthi S. Byadagi ◽  
Sharanappa T. Nandibewoor ◽  
Shrinivas D. Joshi ◽  
Uttam A. More ◽  
...  
Keyword(s):  
Molecular Docking ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Disodium Salt ◽  
In Vitro Studies ◽  
Antibiotic Drug

Investigation of the Effects of Various Cyclodextrins on the Stabilisation of Human Serum Albumin by a Spectroscopic Method

2015 ◽  
Vol 68 (12) ◽  
pp. 1894 ◽  
Author(s):  
Mohsen Oftadeh ◽  
Golamreza Rezaei Behbahani ◽  
Ali Akbar Saboury ◽  
Shahnaz Rafiei
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Electrostatic Interactions ◽  
Spectroscopic Method ◽  
Phosphate Buffer Solution ◽  
Blue Shift ◽  
Titration Calorimetry ◽  
Tryptophan Residue ◽  
Buffer Solution

The binding parameters between cyclodextrins (CDs) and human serum albumin (HSA) were investigated by isothermal titration calorimetry (ITC), fluorescence quenching, and UV-vis absorption spectroscopy at 300 K in 50 mM phosphate buffer solution. Among the various CDs investigated, β-CD has the greater ability to decrease the aggregation of HSA and the results indicated that the inhibition order is γ-CD < α-CD < β-CD. The obtained heats for HSA+CDs interactions were reported and analysed in terms of the extended solvation model, which was used to reproduce the enthalpies of HSA interactions with CDs over a broad range of complex concentrations. The binding constant and thermodynamic parameters were obtained. These suggested that the binding reaction was driven by both enthalpy and entropy, and electrostatic interactions played a major role in the stabilising of HSA. The parameters and reflected the net effect of β-CD on the HSA stability at low and high cyclodextrin concentrations, respectively. The positive values for indicated that β-CD stabilises the HSA structure at low concentrations. The UV absorption intensity of theses complexes increased and a slight red shift was observed in the absorbance wavelength with increasing the CD concentration. The fluorescence intensity of HSA decreased regularly and a slight blue shift was observed for the emission wavelength with increasing CD concentration. The results indicate that the CD complex could quench the fluorescence of HSA and changes the microenvironment of the tryptophan residue.

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