scholarly journals Elucidating the Influences of Size, Surface Chemistry, and Dynamic Flow on Cellular Association of Nanoparticles Made by Polymerization-Induced Self-Assembly

Small ◽  
2018 ◽  
Vol 14 (34) ◽  
pp. 1801702 ◽  
Author(s):  
Song Yang Khor ◽  
Mai N. Vu ◽  
Emily H. Pilkington ◽  
Angus P. R. Johnston ◽  
Michael R. Whittaker ◽  
...  
2020 ◽  
Author(s):  
Zheng Tian

Many long-known but never-quantified properties in chapters of general chemistry have for the first time been quantitatively compared and consistently unified, using the newly introduced geometro-wave (GW) potential of particles (i.e. atoms, molecules, clusters, ions, and nanoparticles). Th GW Potential has helped update the electrochemistry, Lewis acid-base chemistry, redox chemistry, self-assembly, surface chemistry, catalysis, and inter-nanoparticle bonding.


2020 ◽  
Vol MA2020-01 (38) ◽  
pp. 1691-1691
Author(s):  
Nathan Coutard ◽  
Ahmed Ghedjatti ◽  
Sandrine Lyonnard ◽  
Hanako Okuno ◽  
Laure Guetaz ◽  
...  

Coatings ◽  
2019 ◽  
Vol 9 (2) ◽  
pp. 76 ◽  
Author(s):  
Jagoba Iturri ◽  
Alberto Moreno-Cencerrado ◽  
José Toca-Herrera

The well-known bacterial S-layer protein SbpA from Lysinibacillus sphaericus CCM2177 induces spontaneous crystal formation via cooperative self-assembly of the protein subunits into an ordered supramolecular structure. Recrystallization occurs in the presence of divalent cations (i.e., Ca2+) and finally leads to producing smooth 2-D crystalline coatings composed of squared (p4) lattice structures. Among the factors interfering in such a process, the rate of protein supply certainly plays an important role since a limited number of accessible proteins might turn detrimental for film completion. Studies so far have mostly focused on high SbpA concentrations provided under stopped-flow or dynamic-flow conditions, thus omitting the possibility of investigating intermediate states, in which dynamic flow is applied for more critical concentrations of SbpA (i.e., 25, 10, and 5 µg/mL). In this work, we have characterized both physico-chemical and topographical aspects of the assembly and recrystallization of SbpA protein in such low concentration conditions by means of in situ Quartz Crystal Microbalance with Dissipation (QCMD) and atomic force microscopy (AFM) measurements, respectively. On the basis of these experiments, we can confirm how the application of a dynamic flow influences the formation of a closed and crystalline protein film from low protein concentrations (i.e., 10 µg/mL), which otherwise would not be formed.


ACS Nano ◽  
2014 ◽  
Vol 8 (10) ◽  
pp. 9979-9987 ◽  
Author(s):  
Hee-Young Lee ◽  
Sun Hae Ra Shin ◽  
Aaron M. Drews ◽  
Aaron M. Chirsan ◽  
Sean A. Lewis ◽  
...  

1991 ◽  
Vol 237 ◽  
Author(s):  
Troy E. Wilson ◽  
Mark D. Bednarski

We are exploring the requirements for enzyme-catalyzed reactions on small molecules tethered to the surfaces of organic monolayers. Despite considerable effort toward understanding enzymatic processes in solution1, the chemistry of enzymes at interfaces has not been studied. Increasingly sophisticated methods of surface modification, including self-assembly2 and photolithographic3 techniques, raise intriguing prospects for enzymatic surface chemistry. This paper describes our initial investigations of the proteolysis of a dipeptide substrate covalently tethered to the surface of a polydiacetylene film using the enzyme, subtilisin BPN'.


2009 ◽  
Vol 113 (6) ◽  
pp. 2187-2196 ◽  
Author(s):  
Jie Xu ◽  
Mark J. Stevens ◽  
Timothy A. Oleson ◽  
Julie A. Last ◽  
Nita Sahai

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Nita Sahai ◽  
Hussein Kaddour ◽  
Punam Dalai ◽  
Ziqiu Wang ◽  
Garrett Bass ◽  
...  

2017 ◽  
Vol 19 (35) ◽  
pp. 23568-23569 ◽  
Author(s):  
Junbai Li ◽  
Krister Holmberg

Surface chemistry and interface science is about phenomena at interfaces and the self-assembly of amphiphilic molecules.


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