Controlled monolayer self-assembly process based on the atomic force microscopy nanoscratching method

2009 ◽  
Vol 27 (3) ◽  
pp. 1247
Author(s):  
Y. D. Yan ◽  
T. Sun ◽  
B. Pan ◽  
J. W. Zhao ◽  
S. Dong
Keyword(s):  
Atomic Force Microscopy ◽  
Self Assembly ◽  
Assembly Process ◽  
Force Microscopy ◽  
Atomic Force

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.

scholarly journals Morphometric characterization of fibrinogen's αC regions and their role in fibrin self-assembly and molecular organization

Nanoscale ◽  
2017 ◽  
Vol 9 (36) ◽  
pp. 13707-13716 ◽  
Author(s):  
Anna D. Protopopova ◽  
Rustem I. Litvinov ◽  
Dennis K. Galanakis ◽  
Chandrasekaran Nagaswami ◽  
Nikolay A. Barinov ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Self Assembly ◽  
Molecular Organization ◽  
Microscopy Imaging ◽  
Force Microscopy ◽  
Atomic Force ◽  
Atomic Force Microscopy Imaging ◽  
Morphometric Characterization

High-resolution atomic force microscopy imaging reveals the role of fibrinogen αC regions in the early stages of fibrin self-assembly.

The Specific Binding between Galactose Group and Ricinus Communis Agglutinin (RCA) Investigated with Microcantilever

2012 ◽  
Vol 531-532 ◽  
pp. 600-604
Author(s):  
Hui Yong Zhang ◽  
Ji Hu ◽  
Hui Min Liu
Keyword(s):  
Atomic Force Microscopy ◽  
Self Assembly ◽  
Control Experiment ◽  
Ricinus Communis ◽  
Specific Binding ◽  
Specific Interaction ◽  
Protein Layer ◽  
Force Microscopy ◽  
Atomic Force ◽  
Ricinus Communis Agglutinin

The specific recognization between galactose group and Ricinus Communis Agglutinin (RCA) was investigated by microcantilever. The gold side of the microcantilever was covalently bound with N-galactose, RCA and asialofetuin (ASF) via mixed self assembly monolayer of 11-mercaptoundecanoic acid and 6-mercaptohexanol, respectively. After adding RCA into the flowing cell, the deflection could be observed on the N-galactose or ASF modified microcantilever. Meanwhile, the deflection could also be observed after ASF bound to the RCA modified microcantilever. In order to prove that the deflection is caused by the specific interaction between the galactose group and RCA, bovine serum albumin (BSA) was introduced into the flowing cell as control experiment and no obvious deflection was observed. The specific interaction was also confirmed by the evidence that the bound protein layer can be mechanically removed with atomic force microscopy nanolithography technology.

Self-Assembly of Amyloid-Like Peptides at Interfaces Investigated by Atomic Force Microscopy

2017 ◽  
Vol 9 (1) ◽  
pp. 65-76 ◽  
Author(s):  
Haozhi Lei ◽  
Xueqiang Zhang ◽  
Jun Hu ◽  
Yi Zhang
Keyword(s):  
Atomic Force Microscopy ◽  
Self Assembly ◽  
Force Microscopy ◽  
Atomic Force

Self-Assembly of Polyphenylene Dendrimers into Micrometer Long Nanofibers:  An Atomic Force Microscopy Study

Langmuir ◽  
2002 ◽  
Vol 18 (6) ◽  
pp. 2385-2391 ◽  
Author(s):  
Daojun Liu ◽  
Hua Zhang ◽  
P. C. M. Grim ◽  
S. De Feyter ◽  
U.-M. Wiesler ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Self Assembly ◽  
Microscopy Study ◽  
Atomic Force Microscopy Study ◽  
Force Microscopy ◽  
Atomic Force ◽  
Polyphenylene Dendrimers

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.

Role of Oxide Surface Chemistry and Phospholipid Phase on Adsorption and Self-Assembly: Isotherms and Atomic Force Microscopy

2009 ◽  
Vol 113 (6) ◽  
pp. 2187-2196 ◽  
Author(s):  
Jie Xu ◽  
Mark J. Stevens ◽  
Timothy A. Oleson ◽  
Julie A. Last ◽  
Nita Sahai
Keyword(s):  
Atomic Force Microscopy ◽  
Surface Chemistry ◽  
Self Assembly ◽  
Oxide Surface ◽  
Force Microscopy ◽  
Atomic Force
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