Drug-binding to biological macromolecules. A kinetic study of the system chlorodiazepoxide (librium) and bovine serum albumin

1986 ◽  
Vol 18 (10) ◽  
pp. 1123-1132 ◽  
Author(s):  
Edna Nissani ◽  
Berta Perlmutter-Hayman
2009 ◽  
Vol 7 (2) ◽  
pp. 148-152
Author(s):  
Xianjuan Gao ◽  
Yujun Zhang ◽  
Chuntao Zhao ◽  
Xiaolei Sheng ◽  
Ruiyan Zhen

2012 ◽  
Vol 45 (7) ◽  
pp. 520-529 ◽  
Author(s):  
J. Równicka-Zubik ◽  
A. Sułkowska ◽  
M. Maciążek-Jurczyk ◽  
L. Sułkowski ◽  
W. W. Sułkowski

Materials ◽  
2019 ◽  
Vol 12 (7) ◽  
pp. 1022 ◽  
Author(s):  
Jing Yu ◽  
Yun Chen ◽  
Liqun Xiong ◽  
Xiaoyue Zhang ◽  
Yue Zheng

Proteins, due to their binding selectivity, are promising candidates for fabricating nanoscale bio-sensors. However, the influence of structural change on protein conductance caused by specific protein-ligand interactions and disease-induced degeneration still remains unknown. Here, we excavated the relationship between circular dichroism (CD) spectroscopy and conductive atomic force microscopy (CAFM) to reveal the effect of the protein secondary structures changes on conductance. The secondary structure of bovine serum albumin (BSA) was altered by the binding of drugs, like amoxicillin (Amox), cephalexin (Cefa), and azithromycin (Azit). The CD spectroscopy shows that the α-helical and β-sheet content of BSA, which varied according to the molar ratio between the drug and BSA, changed by up to 6%. The conductance of BSA monolayers in varying drug concentrations was further characterized via CAFM. We found that BSA conductance has a monotonic relation with α-helical content. Moreover, BSA conductance seems to be in connection with the binding ability of drugs and proteins. This work elucidates that protein conductance variations caused by secondary structure transitions are triggered by drug-binding and indicate that electrical methods are of potential application in protein secondary structure analysis.


2021 ◽  
pp. 2150028
Author(s):  
Ting Li ◽  
Jialu Yu ◽  
Hao Sui ◽  
Tao Zhang ◽  
Ronghui Zhou

Nanohydroxyapatite (nHAp) has gained considerable concerns due to its vast potential in biomedical applications such as drug delivery, tissue engineering and bone repair. However, the preparation of HAp nanostructures in a controllable manner under environment-friendly reaction conditions remains a challenge. In recent years, the use of biological macromolecules or proteins as templates in the production of nanomaterials has gained more attention due to the relatively mild physical conditions needed for biomimetic synthesis. In this study, a novel nHAp was fabricated by employing bovine serum albumin (BSA) as template under mild condition. After that, the as-obtained nanostructured materials which have well-defined structures and morphologies were characterized by various methods. Furthermore, the rod-like shaped hydroxyapatite demonstrated improved stability properties, as well as cell viability and biocompatibility, compared to BSA free synthesized c-HAp. We expect that this pleasantly novel research will render new insights into the fabrication strategies of nanomaterials and be of practical importance for the expanding biological application.


1986 ◽  
Vol 59 (11) ◽  
pp. 3399-3403 ◽  
Author(s):  
Kiyofumi Murakami ◽  
Yukio Kubota ◽  
Yasuo Fujisaki ◽  
Takayuki Sano

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