Fibrinogen Adsorption on Hydroxyapatite, Carbonate Apatite and Gold Surfaces In Situ Detected by Quartz Crystal Microbalance with Resistance Technique

2012 ◽  
Vol 1418 ◽  
Author(s):  
Hiroshi Yonekura ◽  
Motohiro Tagaya ◽  
Tomohiko Yoshioka ◽  
Toshiyuki Ikoma ◽  
Junzo Tanaka

ABSTRACTWhen a biomaterial is implanted into the body, blood proteins adsorb on its surface and subsequently cells adhere via the protein adlayer. Thus, the understanding of protein adsorption and conformational change on the biomaterial surfaces is of great importance to control the biocompatibility such as antithrombotic properties and cell adhesion behaviors. In this study, we synthesized hydroxyapatite (HAp) and carbonate apatite (CAp) by a wet method. Then we successfully fabricated the HAp and CAp sensors for QCM-R by an electrophoretic deposition method. Adsorption behavior of proteins on the bone substitute material can be monitored by using these apatite sensors. Bovine serum albumin and fibrinogen were employed for the model proteins, and monitored the adsorption behavior on the HAp, CAp and reference gold (Au) sensors by the QCM-R technique. As a result, we revealed that fibrinogen and bovine serum albumin adsorbs on the gold surface by hydrophobic interaction, and adsorbs on the HAp and CAp surfaces mainly by electrostatic force. Besides, we revealed that fibrinogen adsorbs on the Au surface more rigid than on the HAp and CAp surfaces while bovine serum albumin adsorbs on the HAp and CAp surface more rigidly than on the Au surface.

2012 ◽  
Vol 26 (0) ◽  
pp. 23-28 ◽  
Author(s):  
Jumpei Hayashi ◽  
Masakazu Kawashita ◽  
Toshiki Miyazaki ◽  
Masanobu Kamitakahara ◽  
Koji Ioku ◽  
...  

2016 ◽  
Vol 5 (1) ◽  
pp. 331-339 ◽  
Author(s):  
Otávio Augusto Chaves ◽  
Edgar Schaeffer ◽  
Carlos Maurício R. Sant'Anna ◽  
José Carlos Netto-Ferreira ◽  
Dari Cesarin-Sobrinho ◽  
...  

Serum albumin is the most abundant protein in blood plasma; among its functions is the transport of a high variety of drugs in the body. Quinones show several biological and pharmacological activities, such as anti-malarial, antitumor, anti-microbial, anti-inflammatory and anti-parasitic. We report fluorescence and circular dichroism (CD) spectroscopic studies to try to understand the interaction process between α-lapachone (α-LAP) and bovine serum albumin (BSA). Studies using computational methods, such as molecular docking, were performed to identify the main cavity in which this interaction occurs as well as the type of intermolecular interactions between the amino acid residues from albumin and the ligand. The BSA fluorescence quenching by added α-LAP is a static process, indicating an initial association BSA: α-LAP. The Ka and Kb values for the interaction BSA: α-LAP are in the range 105-104 L∙mol-1, indicating a strong binding between these two species. CD data show that there is no significant perturbation on the secondary structure of the protein with binding. The negative ΔGo values are consistent with spontaneous binding occurring endothermically (ΔHo = 127 kJ∙mol-1), and possibly driven by hydrophobic factors (ΔSo = 0.526 kJ∙mol-1∙s-1). The number of binding sites (n) indicates the existence of just one main binding site in BSA for α-LAP, with molecular docking results showing that it binds preferentially to the albumin in the domain IIA, where the Trp-212 residue is located. The ligand interacts via hydrogen bond with Arg-259 and Tyr-149 residues and via T-stacking with the fluorophore Trp-212 residue.


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