Binding of Water‐Soluble CdSe Quantum Dots with Human Serum Albumin: Further Studies into their Effects on Dietary Polyphenol Binding and Sensing of Antibiotic Lomefloxacin

2021 ◽  
Vol 6 (40) ◽  
pp. 11144-11156
Author(s):  
Mahabul Haque ◽  
Sujan Santra ◽  
Debojit Paul ◽  
Atanu Singha Roy
2010 ◽  
Vol 104 (11) ◽  
pp. 1148-1155 ◽  
Author(s):  
Jianbo Xiao ◽  
Tingting Chen ◽  
Longsheng Chen ◽  
Hui Cao ◽  
Fan Yang ◽  
...  

2006 ◽  
Vol 10 (01) ◽  
pp. 33-42 ◽  
Author(s):  
Myriam E. Rodriguez ◽  
Daniel A. Fernández ◽  
Josefina Awruch ◽  
Silvia E. Braslavsky ◽  
Lelia E. Dicelio

The photophysical properties of tetrakis(1,1-dimethyl-2-trimethylammonium)ethylphthalocyaninato zinc(II) tetraiodide (I) – a water-soluble cationic phthalocyanine – are presented in the presence of human serum albumin (HSA) and in micelles of sodium dodecylsulfate ( SDS ) and hexadecyltrimethylammonium chloride ( CTAC ). Spectrophotometric measurements showed that the surfactants SDS and CTAC induce monomerization of I, although the latter less efficiently than the former. This effect is less pronounced in the presence of HSA. The strength of this effect is evaluated through dimerization constants, which are Kd = (5 ± 1) × 105 m−1 in SDS , (1.5 ± 0.5) × 106 M −1 in CTAC , and (1.8 ± 0.9) × 106 M −1 in HSA. Fluorescence experiments confirm that aggregation of I drops as the concentration of surfactant is raised. Triplet quantum yields also decreased upon aggregation and were Φ T = 0.59, 0.16, and < 0.01 in SDS , CTAC , and HSA, respectively. These results indicate that the affinity of I for the environment is not just due to ionic interactions; hydrophobic interactions play an equally important role.


1978 ◽  
Vol 171 (2) ◽  
pp. 453-459 ◽  
Author(s):  
C Jacobsen

Bilirubin can be coupled covalently to albumin by using water-soluble carbodi-imide as coupling reagent. The optimal specificity in the attachment of bilirubin to the high-affinity site on the albumin molecule was obtained by treating an albumin-bilirubin complex with carbodi-imide in low concentrations and for a short period. The product was reduced, carboxymethylated and digested with trypsin. By fractionation on Sephadex G-50 (superfine grade) a peptide fraction containing most of the bilirubin label was isolated. Further purification by paper chromatography gave one peptide, consisting of residues 240-258. The peptide containined a single lysine residue, 240, and had an intact disulphide bridge. The results indicate that bilirubin is bound to lysine residue 240 at its high-affinity site on human serum albumin.


2010 ◽  
Vol 12 (3) ◽  
pp. 349-364 ◽  
Author(s):  
Graziano Colombo ◽  
Giancarlo Aldini ◽  
Marica Orioli ◽  
Daniela Giustarini ◽  
Rosalba Gornati ◽  
...  

Author(s):  
Xuan Ma ◽  
Lusha Liu ◽  
Xuhua Liang ◽  
Bo Zhao ◽  
Lin Shi ◽  
...  

ChemPhysChem ◽  
2020 ◽  
Vol 21 (24) ◽  
pp. 2709-2714 ◽  
Author(s):  
Sucheta Banerjee ◽  
Tanuja Kistwal ◽  
Amritha Sajeevan ◽  
Anindya Datta

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