scholarly journals Startling temperature effect on proteins when confined: single molecular level behaviour of human serum albumin in a reverse micelle

2016 ◽  
Vol 18 (21) ◽  
pp. 14350-14358 ◽  
Author(s):  
Bhaswati Sengupta ◽  
Rajeev Yadav ◽  
Pratik Sen
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Fluorescence Correlation Spectroscopy ◽  
Molecular Level ◽  
Correlation Spectroscopy ◽  
Fluorescence Correlation ◽  
Conformational Fluctuation ◽  
Fluctuation Dynamics ◽  
Domain I

The present work reports the effect of confinement, and temperature therein, on the conformational fluctuation dynamics of domain-I of human serum albumin (HSA) by fluorescence correlation spectroscopy (FCS).

Effect of an Ionic liquid on the Unfolding of Human Serum Albumin: A Fluorescence Correlation Spectroscopy Study

ChemPhysChem ◽  
2011 ◽  
Vol 13 (7) ◽  
pp. 1949-1955 ◽  
Author(s):  
Dibyendu Kumar Das ◽  
Atanu Kumar Das ◽  
Amit Kumar Mandal ◽  
Tridib Mondal ◽  
Kankan Bhattacharyya
Keyword(s):  
Ionic Liquid ◽  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Fluorescence Correlation Spectroscopy ◽  
Correlation Spectroscopy ◽  
Spectroscopy Study ◽  
Fluorescence Correlation

scholarly journals Effects of surface functionalization on the adsorption of human serum albumin onto nanoparticles – a fluorescence correlation spectroscopy study

2014 ◽  
Vol 5 ◽  
pp. 2036-2047 ◽  
Author(s):  
Pauline Maffre ◽  
Stefan Brandholt ◽  
Karin Nienhaus ◽  
Li Shang ◽  
Wolfgang J Parak ◽  
...  
Keyword(s):  
Human Serum Albumin ◽  
Serum Albumin ◽  
Human Serum ◽  
Fluorescence Correlation Spectroscopy ◽  
Pt Nanoparticles ◽  
Protein Corona ◽  
Correlation Spectroscopy ◽  
Surface Charges ◽  
Fluorescence Correlation ◽  
Coulombic Interactions

By using fluorescence correlation spectroscopy (FCS), we have studied the adsorption of human serum albumin (HSA) onto Fe–Pt nanoparticles (NPs, 6 nm radius), CdSe/ZnS quantum dots (QDs, 5 nm radius) and Au and Ag nanoclusters (1–4 nm radius), which are enshrouded by various water-solubilizing surface layers exposing different chemical functional groups (carboxyl, amino and both), thereby endowing the NPs with different surface charges. We have also measured the effects of modified surface functionalizations on the protein via succinylation and amination. A step-wise increase in hydrodynamic radius with protein concentration was always observed, revealing formation of protein monolayers coating the NPs, independent of their surface charge. The differences in the thickness of the protein corona were rationalized in terms of the different orientations in which HSA adsorbs onto the NPs. The midpoints of the binding transition, which quantifies the affinity of HSA toward the NP, were observed to differ by almost four orders of magnitude. These variations can be understood in terms of specific Coulombic interactions between the proteins and the NP surfaces.

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