Insights into the structural changes of bovine serum albumin in ethanolammonium laurate based surface active ionic liquids

2019 ◽  
Vol 290 ◽  
pp. 111229 ◽  
Author(s):  
Anu Aravind Thoppil ◽  
Bharath Kumar Chennuri ◽  
Ramesh L. Gardas
2020 ◽  
pp. 114537
Author(s):  
Márcia M.S. Alves ◽  
João M.M. Araújo ◽  
Ivo C. Martins ◽  
Ana B. Pereiro ◽  
Margarida Archer

RSC Advances ◽  
2020 ◽  
Vol 10 (12) ◽  
pp. 7073-7082
Author(s):  
Gagandeep Singh ◽  
Manvir Kaur ◽  
Vinod Kumar Aswal ◽  
Tejwant Singh Kang

Physicochemical and computational investigation of complexation between BSA and SAILs with application in material transport.


2012 ◽  
Vol 116 (39) ◽  
pp. 11924-11935 ◽  
Author(s):  
Tejwant Singh ◽  
Pankaj Bharmoria ◽  
Masa-aki Morikawa ◽  
Nobuo Kimizuka ◽  
Arvind Kumar

2009 ◽  
Vol 103 (12) ◽  
pp. 1729-1738 ◽  
Author(s):  
Giovanna Navarra ◽  
Anna Tinti ◽  
Maurizio Leone ◽  
Valeria Militello ◽  
Armida Torreggiani

2017 ◽  
Vol 41 (19) ◽  
pp. 10712-10722 ◽  
Author(s):  
Lakkoji Satish ◽  
Sabera Millan ◽  
Krishnendu Bera ◽  
Sujata Mohapatra ◽  
Harekrushna Sahoo

Experimental and theoretical evidence in support of the stabilizing effect of ammonium-based ionic liquids on thermal unfolding/refolding of bovine serum albumin is provided in this article.


Molecules ◽  
2019 ◽  
Vol 25 (1) ◽  
pp. 90 ◽  
Author(s):  
Paula Ossowicz ◽  
Proletina Kardaleva ◽  
Maya Guncheva ◽  
Joanna Klebeko ◽  
Ewelina Świątek ◽  
...  

The development of ionic liquids based on active pharmaceutical ingredients (API-ILs) is a possible solution to some of the problems of solid and/or hydrophobic drugs such as low solubility and bioavailability, polymorphism and an alternative route of administration could be suggested as compared to the classical drug. Here, we report for the first time the synthesis and detailed characterization of a series of ILs containing a cation amino acid esters and anion ketoprofen (KETO-ILs). The affinity and the binding mode of the KETO-ILs to bovine serum albumin (BSA) were assessed using fluorescence spectroscopy. All compounds bind in a distance not longer than 6.14 nm to the BSA fluorophores. The estimated binding constants (KA) are in order of 105 L mol−1, which is indicative of strong drug or IL-BSA interactions. With respect to the ketoprofen-BSA system, a stronger affinity of the ILs containing l-LeuOEt, l-ValOBu, and l-ValOEt cation towards BSA is clearly seen. Fourier transformed infrared spectroscopy experiments have shown that all studied compounds induced a rearrangement of the protein molecule upon binding, which is consistent with the suggested static mechanism of BSA fluorescence quenching and formation of complexes between BSA and the drugs. All tested compounds were safe for macrophages.


2012 ◽  
Vol 132 (3) ◽  
pp. 622-628 ◽  
Author(s):  
Hua Yan ◽  
Junyong Wu ◽  
Guoliang Dai ◽  
Aiguo Zhong ◽  
Hao Chen ◽  
...  

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