scholarly journals Immunoactivity of self-assembled antibodies investigated by atomic force microscopy

RSC Advances ◽  
2018 ◽  
Vol 8 (51) ◽  
pp. 29378-29384 ◽  
Author(s):  
Hiroaki Kominami ◽  
Kei Kobayashi ◽  
Shinichiro Ido ◽  
Hirokazu Kimiya ◽  
Hirofumi Yamada
Keyword(s):  
Atomic Force Microscopy ◽  
Self Assembly ◽  
The Self ◽  
Two Dimensional ◽  
Igg Antibodies ◽  
Association Rate Constant ◽  
Association Rate ◽  
Force Microscopy ◽  
Atomic Force ◽  
Self Assembled

We investigated self-assembly such as hexamerization and two-dimensional crystallization of immunoglobulin G (IgG) molecules on mica by atomic force microscopy. We also estimated the association rate constant of the self-assembled IgG antibodies.

Self-Assembled Lipid Tubules: Synthesis, Characterization, and Ordered Arrays

2006 ◽  
Vol 922 ◽  
Author(s):  
Yue Zhao ◽  
Nidhi Mahajan ◽  
Jiyu Fang
Keyword(s):  
Atomic Force Microscopy ◽  
Lipid Bilayer ◽  
Surface Patterning ◽  
The Self ◽  
Two Dimensional ◽  
Force Microscopy ◽  
Ordered Arrays ◽  
Atomic Force ◽  
Self Assembled ◽  
Lipid Tubules

AbstractThe rolling of lipid bilayer sheets into hollow cylindrical tubules have emerged as a group of interesting supramolecular nanostructures. Here, we image the self-assembled tubules of 1,2-bis(tricosa-10,12-diynoyl)-sn-glycero-3-phosphochloline (DC8,9PC) with atomic force microscopy. Nanoscale ripple structures with a periodicity of ~ 200nm in the cylindrical lipid tubules are observed. We develop two simple methods based on microfluidic networks and surface patterning to produce two dimensional ordered arrays of parallel aligned lipid tubules on substrates.

NANOSTRUCTURES FROM DESIGNER PEPTIDES

COSMOS ◽  
2008 ◽  
Vol 04 (02) ◽  
pp. 173-183
Author(s):  
BOON TEE ONG ◽  
PARAYIL KUMARAN AJIKUMAR ◽  
SURESH VALIYAVEETTIL
Keyword(s):  
Atomic Force Microscopy ◽  
Solid State ◽  
Self Assembly ◽  
Size Range ◽  
The Self ◽  
Mica Surface ◽  
Force Microscopy ◽  
Solution Structures ◽  
Atomic Force

The present article reviews the self-assembly of oligopeptides to form nanostructures, both in solution and in solid state. The solution structures of the peptides were examined using circular dichroism and dynamic light scattering. The solid state assembly was examined by adsorbing the peptides onto a mica surface and analyzing it using atomic force microscopy. The role of pH and salt concentration on the peptide self-assembly was also examined. Nanostructures within a size range of 3–10 nm were obtained under different conditions.

scholarly journals Cation-Specific Effects on the Self-Assembly of Collagen Molecules Mediated by Acetate on Mica Surface Observed with Atomic Force Microscopy

2017 ◽  
Vol 2017 ◽  
pp. 1-10 ◽  
Author(s):  
Zhiwei Wang ◽  
Qi Xiao ◽  
Xuan Song ◽  
Yunfei Wan ◽  
Jie Zhu
Keyword(s):  
Atomic Force Microscopy ◽  
Self Assembly ◽  
Ionic Concentration ◽  
Collagen Fibrils ◽  
The Self ◽  
Mica Surface ◽  
Force Microscopy ◽  
Specific Effects ◽  
Atomic Force ◽  
Base Method

The well-organized collagen layers on mica surface have drawn extensive attention for its essential applications and studies on the process of self-assembly as a model system. In this work, collagen extracted from fish scales by acid-base method was used to explore the self-assembly characters, and atomic force microscopy was applied to observe the collagen assembled on mica surface mediated by acetate with four different cations, including K+, Na+, Mg2+, and Ca2+. It showed that cations might influence the interaction between collagen fibrils and mica surface at high ionic concentration. And a similar network structure was acquired with uniform pore size for four kinds of acetates; nearly ranged collagen fibrils in the same direction were collected in Mg2+ solutions, while flat films with some fibrils were achieved in K+ solutions. The Hofmeister series and Collins’ model were adapted to explain the effects of cations and acetate on the self-assembly of collagen. These results and analysis would be helpful for directing the pattern of collagen assembly on a solid surface with a potential application in food science and engineering.

Morphology of Self-Assembled InAs Quantum Dots on GaAs(001)

2001 ◽  
Vol 696 ◽  
Author(s):  
F. Arciprete ◽  
F. Patella ◽  
M. Fanfoni ◽  
S. Nufris ◽  
E. Placidi ◽  
...  
Keyword(s):  
Nucleation And Growth ◽  
The Self ◽  
Two Dimensional ◽  
Wetting Layer ◽  
Inas Quantum Dots ◽  
Initial Formation ◽  
Force Microscopy ◽  
Atomic Force ◽  
Self Assembled

AbstractWe have followed by Atomic Force Microscopy (AFM) the epitaxial growth of InAs on GaAs(001) starting from the initial formation of a strained two-dimensional wetting layer up to the self-assembled nucleation and growth of 3D nanoparticles. In this work we underline many aspects of the morphology of this system, which substantiate the role either of kinetics on thermodynamics in the process of growth as well as the role of surface instabilities in controlling lateral ordering of the nanoaggregates.

scholarly journals Self-assembly and wetting properties of gold nanorod–CTAB molecules on HOPG

2019 ◽  
Vol 10 ◽  
pp. 696-705 ◽  
Author(s):  
Imtiaz Ahmad ◽  
Floor Derkink ◽  
Tim Boulogne ◽  
Pantelis Bampoulis ◽  
Harold J W Zandvliet ◽  
...  
Keyword(s):  
Self Assembly ◽  
Cetyltrimethylammonium Bromide ◽  
Pyrolytic Graphite ◽  
The Self ◽  
Gold Nanorod ◽  
Force Microscopy ◽  
Wetting Properties ◽  
Atomic Force ◽  
Highly Ordered Pyrolytic Graphite ◽  
Self Assembled

The formation of self-assembled superstructures of cetyltrimethylammonium bromide (CTAB) after drying on a nonwetting highly ordered pyrolytic graphite (HOPG) surface have been investigated using scanning electron microscopy (SEM) and atomic force microscopy (AFM). Although SEM did not reveal coverage of CTAB layers, AFM showed not only CTAB assembly, but also the dynamics of the process on the surface. The self-assembled layers of CTAB molecules on the HOPG terraces prior to nanorod deposition were shown to change the wettability of the surface, and as a result, gold nanorod deposition takes place on nonwetting HOPG terraces.

scholarly journals Observing Effects of Calcium/Magnesium Ions and pH Value on the Self-Assembly of Extracted Swine Tendon Collagen by Atomic Force Microscopy

2017 ◽  
Vol 2017 ◽  
pp. 1-8 ◽  
Author(s):  
Xuan Song ◽  
Zhiwei Wang ◽  
Shiyu Tao ◽  
Guixia Li ◽  
Jie Zhu
Keyword(s):  
Atomic Force Microscopy ◽  
Metal Ions ◽  
Self Assembly ◽  
Food Packaging ◽  
Ph Value ◽  
The Self ◽  
Solution Ph ◽  
Collagen Concentration ◽  
Force Microscopy ◽  
Atomic Force

Self-assembly of extracted collagen from swine trotter tendon under different conditions was firstly observed using atomic force microscopy; then the effects of collagen concentration, pH value, and metal ions to the topography of the collagen assembly were analyzed with the height images and section analysis data. Collagen assembly under 0.1 M, 0.2 M, 0.3 M CaCl2, and MgCl2 solutions in different pH values showed significant differences (P < 0.05) in the topographical properties including height, width, and roughness. With the concentration being increased, the width of collagen decreased significantly (P < 0.05). The width of collagen fibers was first increased significantly (P < 0.05) and then decreased with the increasing of pH. The collagen was assembled with network structure on the mica in solution with Ca2+ ions. However, it had shown uniformed fibrous structure with Mg2+ ions on the new cleaved mica sheet. In addition, the width of collagen fibrous was 31~58 nm in solution with Mg2+ but 21~50 nm in Ca2+ solution. The self-assembly collagen displayed various potential abilities to construct fibers or membrane on mica surfaces with Ca2+ ions and Mg2+ irons. Besides, the result of collagen self-assembly had shown more relations among solution pH value, metal ions, and collagen molecular concentration, which will provide useful information on the control of collagen self-assembly in tissue engineering and food packaging engineering.

Dynamic Self-Assembly Process of a Designed Peptide

2013 ◽  
Vol 750-752 ◽  
pp. 1630-1634
Author(s):  
Li Ping Ruan ◽  
Zhi Hua Xing
Keyword(s):  
Atomic Force Microscopy ◽  
Self Assembly ◽  
The Self ◽  
Layer By Layer ◽  
Assembly Process ◽  
Force Microscopy ◽  
Atomic Force ◽  
Sheet Structure ◽  
Β Sheet ◽  
Layer Assembly

In this paper, we reported the dynamic self-assembly process of an half-sequence ionic self-complementarity peptide CH3CO-Pro-Ser-Phe-Cys-Phe-Lys-Phe-Glu-Pro-NH2, which could self-assemble into stable nanofibers and formed hydrogel consisting of >99% water. The dynamic self-assembly process was detected by circular dichroism (CD) and atomic force microscopy (AFM). CD spectrum revealed that the mainly contents of the peptide were regular β-sheet structure. The data indicated that though the secondary structure of the peptide formed immediately, the microstructure of the self-assembly process of the designed peptide formed slowly. AFM image illustrated that the self-assembly process was layer-by-layer assembly.

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