Interaction of Bovine Serum Albumin and Human Blood Plasma with PEO-Tethered Surfaces:  Influence of PEO Chain Length, Grafting Density, and Temperature

Langmuir ◽  
2004 ◽  
Vol 20 (10) ◽  
pp. 4162-4167 ◽  
Author(s):  
Willem Norde ◽  
Dick Gage
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Blood Plasma ◽  
Chain Length ◽  
Human Blood ◽  
Bovine Serum ◽  
Human Blood Plasma ◽  
Grafting Density

scholarly journals Human blood plasma factors affect the adhesion kinetics of Staphylococcus aureus to central venous catheters

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Gubesh Gunaratnam ◽  
Christian Spengler ◽  
Simone Trautmann ◽  
Philipp Jung ◽  
Johannes Mischo ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Serum Albumin ◽  
Blood Plasma ◽  
Human Blood ◽  
Central Venous Catheters ◽  
Human Blood Plasma ◽  
Adhesion Forces ◽  
Central Venous ◽  
Major Step ◽  
Initial Adhesion

AbstractStaphylococcus aureus is a common cause of catheter-related blood stream infections (CRBSI). The bacterium has the ability to form multilayered biofilms on implanted material, which usually requires the removal of the implanted medical device. A first major step of this biofilm formation is the initial adhesion of the bacterium to the artificial surface. Here, we used single-cell force spectroscopy (SCFS) to study the initial adhesion of S. aureus to central venous catheters (CVCs). SCFS performed with S. aureus on the surfaces of naïve CVCs produced comparable maximum adhesion forces on three types of CVCs in the low nN range (~ 2–7 nN). These values were drastically reduced, when CVC surfaces were preincubated with human blood plasma or human serum albumin, and similar reductions were observed when S. aureus cells were probed with freshly explanted CVCs withdrawn from patients without CRBSI. These findings indicate that the initial adhesion capacity of S. aureus to CVC tubing is markedly reduced, once the CVC is inserted into the vein, and that the risk of contamination of the CVC tubing by S. aureus during the insertion process might be reduced by a preconditioning of the CVC surface with blood plasma or serum albumin.

scholarly journals Internalization, cytotoxicity, oxidative stress and inflammation of multi-walled carbon nanotubes in human endothelial cells: influence of pre-incubation with bovine serum albumin

RSC Advances ◽  
2018 ◽  
Vol 8 (17) ◽  
pp. 9253-9260 ◽  
Author(s):  
Jimin Long ◽  
Xianqiang Li ◽  
Yang Kang ◽  
Yanhuai Ding ◽  
Zhipeng Gu ◽  
...  
Keyword(s):  
Oxidative Stress ◽  
Carbon Nanotubes ◽  
Endothelial Cells ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Human Blood ◽  
Bovine Serum ◽  
Human Endothelial Cells ◽  
Multi Walled Carbon Nanotubes ◽  
Walled Carbon Nanotubes

When entering circulation, multi-walled carbon nanotubes (MWCNTs) will inevitably adsorb proteins, which can consequently influence their toxicity to cells lining human blood vessels.

Antioxidant, Antidiabetic and Anticancer Activities of L-Phenylalanine and L-Tyrosine Ester Surfactants: In Vitro and In Silico Studies of their Interactions with Macromolecules as Plausible Mode of Action for their Biological Properties

2020 ◽  
Vol 15 (6) ◽  
pp. 610-622 ◽  
Author(s):  
Nausheen Joondan ◽  
Sabina J. Laulloo ◽  
Prakashanand Caumul ◽  
Prashant S. Kharkar
Keyword(s):  
Molecular Docking ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Chain Length ◽  
Inhibitory Activity ◽  
Bovine Serum ◽  
Biological Properties ◽  
Docking Studies ◽  
Anticancer Activities ◽  
Binding Studies

Background: Aromatic amino acid-based surfactants have been found to have interesting biological properties such as antibacterial and hemolytic activities. Recently, we have reported the antibacterial activity of a range of ester hydrochloride surfactants derived from L-Phenylalanine and LTyrosine. This study aims at assessing the antioxidant, α-glycosidase inhibitory and cytotoxic activities of a series of L-Phenylalanine and L-Tyrosine ester hydrochlorides. Molecular docking and BSA binding studies were also carried out in order to investigate their potential therapeutic targets. Methods: L-Phenylalanine and L-Tyrosine surfactants were tested as potential lipophilic antioxidants using the DPPH and ABTS assays. These surfactants were also tested for their α-glycosidase inhibitory activity using 4-nitrophenyl α -D-glucopyranoside (pNPG) as substrate. Their cytotoxicity effects were screened using HeLa and KB cell lines. Glide version 5.7 as implemented in Schrödinger suite 2013-1, was used for performing docking studies of L-Phenylalanine and L-Tyrosine dodecyl esters. The interaction of the ester hydrochlorides of L-Phenylalanine and L-Tyrosine with bovine serum albumin (BSA) was investigated using fluorometric titration. Results: The presence of the phenolic moiety in L-Tyrosine-based surfactants was found to enhance the antioxidant and α-glucosidase inhibitory activities compared to the L-Phenylalanine derivatives. The α- glucosidase and anticancer activities of the phenylalanine surfactants were found to increase with chain length up to C12 above which the activities exhibited a downward trend. In the case of the tyrosine series, an increase in chain length from C8 to C14 was found to decrease the α-glucosidase inhibitory activity and increase the anticancer activity of the surfactants. Binding studies with bovine serum albumin showed that the tyrosine surfactants displayed greater affinity for the serum albumin, owing to the presence of the phenolic group which altered the orientation of the surfactant molecule within the hydrophobic core of BSA. Conclusion: L-Tyrosine esters having a phenolic moiety were found to possess enhanced biological activity in terms of both the antioxidant and antidiabetic activities as well as also bind more strongly to Bovine serum albumin. Molecular docking studies of the phenylalanine and tyrosine surfactants of similar chain length with target proteins showed direct correlation with their anticancer and antidiabetic activity. Therefore, the findings show that these aromatic based surfactants derived from L-Tyrosine can act as promising antioxidant, antidiabetic and anticancer agents, and they can also be efficiently transported and eliminated in the body, making them useful candidates for drug designs.

The effects of ligand chain length, salt concentration and temperature on the adsorption of bovine serum albumin onto polypropyleneglycol-Sepharose

2005 ◽  
Vol 19 (8) ◽  
pp. 606-616 ◽  
Author(s):  
A. C. Dias-Cabral ◽  
A. S. Ferreira ◽  
J. Phillips ◽  
J. A. Queiroz ◽  
N. G. Pinto
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Chain Length ◽  
Salt Concentration ◽  
Bovine Serum
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