PNIPAmx–PPO36–PNIPAmx thermo-sensitive triblock copolymers: chain conformation and adsorption behavior on a hydrophobic gold surface

2016 ◽  
Vol 18 (1) ◽  
pp. 519-528 ◽  
Author(s):  
Jianyuan Li ◽  
Zhijun Zhang ◽  
Xianjing Zhou ◽  
Tongquan Chen ◽  
Jingjing Nie ◽  
...  

The presence of the PNIPAm block is not a sufficient condition for the complex adsorption behavior of PNIPAmx–PPO36–PNIPAmx triblock copolymers.

Langmuir ◽  
2009 ◽  
Vol 25 (8) ◽  
pp. 4484-4489 ◽  
Author(s):  
Chris S. Hodges ◽  
Simon Biggs ◽  
Lynn Walker

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.


2019 ◽  
Vol 123 (15) ◽  
pp. 9860-9867
Author(s):  
Bertram Schulze Lammers ◽  
René Ebeling ◽  
Elena Dirksen ◽  
Thomas J. J. Müller ◽  
Silvia Karthäuser

Author(s):  
John H. Luft

With information processing devices such as radio telescopes, microscopes or hi-fi systems, the quality of the output often is limited by distortion or noise introduced at the input stage of the device. This analogy can be extended usefully to specimen preparation for the electron microscope; fixation, which initiates the processing sequence, is the single most important step and, unfortunately, is the least well understood. Although there is an abundance of fixation mixtures recommended in the light microscopy literature, osmium tetroxide and glutaraldehyde are favored for electron microscopy. These fixatives react vigorously with proteins at the molecular level. There is clear evidence for the cross-linking of proteins both by osmium tetroxide and glutaraldehyde and cross-linking may be a necessary if not sufficient condition to define fixatives as a class.


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