Investigation of the Differences in Thermal Stability of Two Recombinant Human Serum Albumins with 1,2-Dipalmitoyl-sn-glycero-3-phosphocholine Liposomes by UV Circular Dichroism Spectropolarimetry

2012 ◽  
Vol 116 (15) ◽  
pp. 4661-4670 ◽  
Author(s):  
Grant E. Frahm ◽  
Terry D. Cyr ◽  
Daryl G. S. Smith ◽  
Lisa D. Walrond ◽  
Michael J. W. Johnston
Keyword(s):  
Thermal Stability ◽  
Circular Dichroism ◽  
Human Serum ◽  
Serum Albumins ◽  
Circular Dichroïsm ◽  
Thermal Stability Of

Influence of Glycerol on the Structure and Thermal Stability of Lysozyme: A Dynamic Light Scattering and Circular Dichroism Study

2009 ◽  
Vol 113 (51) ◽  
pp. 16420-16424 ◽  
Author(s):  
Alessandro Esposito ◽  
Lucia Comez ◽  
Stefania Cinelli ◽  
Filippo Scarponi ◽  
Giuseppe Onori
Keyword(s):  
Thermal Stability ◽  
Circular Dichroism ◽  
Light Scattering ◽  
Dynamic Light Scattering ◽  
Circular Dichroïsm ◽  
Thermal Stability Of

scholarly journals Thermal Stability of Heterotrimeric pMHC Proteins as Determined by Circular Dichroism Spectroscopy

BIO-PROTOCOL ◽  
2017 ◽  
Vol 7 (13) ◽  
Author(s):  
Anna Fuller ◽  
Aaron Wall ◽  
Michael Crowther ◽  
Angharad Lloyd ◽  
Alexei Zhurov ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Circular Dichroism ◽  
Circular Dichroism Spectroscopy ◽  
Circular Dichroïsm ◽  
Thermal Stability Of

scholarly journals Interaction of the Coffee Diterpenes Cafestol and 16-O-Methyl-Cafestol Palmitates with Serum Albumins

2020 ◽  
Vol 21 (5) ◽  
pp. 1823
Author(s):  
Federico Berti ◽  
Luciano Navarini ◽  
Elena Guercia ◽  
Ana Oreški ◽  
Alessandra Gasparini ◽  
...  
Keyword(s):  
Circular Dichroism ◽  
Fatty Acid ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Biologically Active ◽  
Aliphatic Chain ◽  
Serum Albumins ◽  
Complex Behaviour ◽  
Circular Dichroïsm

The main coffee diterpenes cafestol, kahweol, and 16-O-methylcafestol, present in the bean lipid fraction, are mostly esterified with fatty acids. They are believed to induce dyslipidaemia and hypercholesterolemia when taken with certain types of coffee brews. The study of their binding to serum albumins could help explain their interactions with biologically active xenobiotics. We investigated the interactions occurring between cafestol and 16-O-methylcafestol palmitates with Bovine Serum Albumin (BSA), Human Serum Albumin (HSA), and Fatty Free Human Serum Albumin (ffHSA) by means of circular dichroism and fluorimetry. Circular Dichroism (CD) revealed a slight change (up to 3%) in the secondary structure of fatty-free human albumin in the presence of the diterpene esters, suggesting that the aliphatic chain of the palmitate partly occupies one of the fatty acid sites of the protein. A warfarin displacement experiment was performed to identify the binding site, which is probably close but not coincident with Sudlow site I, as the affinity for warfarin is enhanced. Fluorescence quenching titrations revealed a complex behaviour, with Stern–Volmer constants in the order of 103–104 Lmol−1. A model of the HSA-warfarin-cafestol palmitate complex was obtained by docking, and the most favourable solution was found with the terpene palmitate chain inside the FA4 fatty acid site and the cafestol moiety fronting warfarin at the interface with site I.

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