A study of the unfolding process of human serum albumin in the acidic pH region by two-dimensional infrared correlation spectroscopy

2000 ◽  
Author(s):  
Koichi Murayama
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Correlation Spectroscopy ◽  
Acidic Ph ◽  
Two Dimensional

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.

Two-Dimensional Attenuated Total Reflection/Infrared Correlation Spectroscopy Studies on Concentration and Heat-Induced Structural Changes of Human Serum Albumin in Aqueous Solutions

2002 ◽  
Vol 56 (9) ◽  
pp. 1186-1193 ◽  
Author(s):  
Yuqing Wu ◽  
Koichi Murayama ◽  
Boguslawa Czarnik-Matusewicz ◽  
Yukihiro Ozaki
Keyword(s):  
Secondary Structure ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Aqueous Solutions ◽  
Ir Spectra ◽  
Total Reflection ◽  
Attenuated Total Reflection ◽  
Correlation Spectroscopy ◽  
Random Coil ◽  
Two Dimensional

Attenuated total reflection (ATR)/FT-IR spectra were measured for human serum albumin (HSA) in aqueous solutions (pH 6.6) with concentrations of 1.0, 2.0, 3.0, 4.0, and 5.0 wt % over a temperature range of 45–80 °C. Generalized two-dimensional (2D) correlation spectroscopy was employed to explore concentration and heat-induced structural variations of HSA in aqueous solutions. To generate 2D correlation spectra, the raw spectra were subjected to the appropriate pretreatment procedure involving ATR correction, subtraction of the spectrum of an aqueous solution, and smoothing. The synchronous and asynchronous correlation spectra were calculated for the concentration-dependent IR spectral variations in the amide I region at various temperatures. The two-dimensional ATR/IR correlation spectra greatly enhance band separation in the region and provide information about the correlation between the amide bands of HSA arising from the same and different secondary structure components. Based on the correlation investigated and previously proposed relationship between the secondary structure elements and the amide band frequencies, we have proposed the detailed assignments in the amide I region at 45 and 80 °C. The proposed assignments are compared with those based on the results of second derivative and Fourier self-deconvolution (FSD) of the ATR/IR spectra. The asynchronous spectrum generated from the concentration-dependent spectral variations at 45 °C show that side chains, the random coil, and extended chains are more sensitive than the α-helices and β-turns to the concentration change. On the other hand, the corresponding spectrum at 80 °C reveals that the conformation changes in side chains and β-turns (or β-strands) of HSA start before those in extended chain, random coil structures, and α-helices.

Two-dimensional gel electrophoresis and immunoblotting of human serum albumin modified by reaction with penicillins

1995 ◽  
Vol 16 (1) ◽  
pp. 851-853 ◽  
Author(s):  
Barbara Marzocchi ◽  
Barbara Magi ◽  
Luca Bini ◽  
Carla Cellesi ◽  
Aldo Rossolini ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Gel Electrophoresis ◽  
Two Dimensional ◽  
Two Dimensional Gel Electrophoresis

Inhibition of Human Serum Albumin Fibrillation by Two-Dimensional Nanoparticles

2017 ◽  
Vol 121 (22) ◽  
pp. 5474-5482 ◽  
Author(s):  
Sudipta Bag ◽  
Rishav Mitra ◽  
Sunando DasGupta ◽  
Swagata Dasgupta
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Two Dimensional

Investigation of DMSO-Induced Conformational Transitions in Human Serum Albumin Using Two-Dimensional Raman Optical Activity Spectroscopy

Chirality ◽  
2014 ◽  
Vol 26 (9) ◽  
pp. 497-501 ◽  
Author(s):  
Andrea N. L. Batista ◽  
João M. Batista ◽  
Lorna Ashton ◽  
Vanderlan S. Bolzani ◽  
Maysa Furlan ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Optical Activity ◽  
Conformational Transitions ◽  
Two Dimensional ◽  
Raman Optical Activity
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