In vitro interaction investigation between three Ru(ii) arene complexes and human serum albumin: structural influences

RSC Advances ◽  
2016 ◽  
Vol 6 (52) ◽  
pp. 47043-47054 ◽  
Author(s):  
Shan Huang ◽  
Shushu Peng ◽  
Wei Su ◽  
Zhaofeng Tang ◽  
Jianguo Cui ◽  
...  

In vitro interactions between three Ru(ii) arene complexes and human serum albumin were systematically investigated by multi-spectroscopic techniques.

2022 ◽  
Vol 146 ◽  
pp. 112513
Author(s):  
Erzsébet Pászti-Gere ◽  
Anna Szentkirályi ◽  
Zsófia Fedor ◽  
Gábor Nagy ◽  
Zoltán Szimrók ◽  
...  

2016 ◽  
Vol 148 ◽  
pp. 165-172 ◽  
Author(s):  
Shan Huang ◽  
Hangna Qiu ◽  
Yi Liu ◽  
Chusheng Huang ◽  
Jiarong Sheng ◽  
...  

2021 ◽  
pp. 116888
Author(s):  
Fahad A. Alhumaydhi ◽  
Mohammad Abdullah Aljasir ◽  
Abdullah S.M. Aljohani ◽  
Suliman A. Alsagaby ◽  
Ameen S.S. Alwashmi ◽  
...  

2020 ◽  
Vol 14 (1) ◽  
pp. 22
Author(s):  
Kenji Tsukigawa ◽  
Shuhei Imoto ◽  
Keishi Yamasaki ◽  
Koji Nishi ◽  
Toshihiko Tsutsumi ◽  
...  

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.


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

RSC Advances ◽  
2014 ◽  
Vol 4 (28) ◽  
pp. 14335-14347 ◽  
Author(s):  
Raina Thakur ◽  
Anupam Das ◽  
Anjan Chakraborty

The interaction of human serum albumin (HSA) with liposomes made of saturated and unsaturated phosphocholines has been studied using circular dichroism (CD), steady state and time resolved fluorescence spectroscopic techniques.


1985 ◽  
Vol 226 (1) ◽  
pp. 251-258 ◽  
Author(s):  
S Itoh ◽  
S Onishi

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.


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