Characterization of Hydrophobic Forces for in Liquid Self-Assembly of Micron-Sized Functional Building Blocks

2011 ◽  
Vol 1299 ◽  
Author(s):  
M. R. Gullo ◽  
L. Jacot-Descombes ◽  
L. Aeschimann ◽  
J. Brugger
Keyword(s):  
Atomic Force Microscopy ◽  
Self Assembly ◽  
Hydrophobic Interactions ◽  
Numerical Study ◽  
Building Blocks ◽  
Dynamic Simulations ◽  
Hydrophobic Force ◽  
Force Microscopy ◽  
Molecular Arrangement ◽  
Atomic Force

ABSTRACTThis paper presents the experimental and numerical study of hydrophobic interaction forces at nanometer scale in the scope of engineering micron-sized building blocks for self-assembly in liquid. The hydrophobic force distance relation of carbon, Teflon and dodeca-thiols immersed in degassed and deionized water has been measured by atomic force microscopy. Carbon and dodeca-thiols showed comparable attractive and binding forces in the rage of pN/nm2. Teflon showed the weakest binding and no attractive force. Molecular dynamic simulations were performed to correlate the molecular arrangement of water molecules and the hydrophobic interactions measured by atomic force microscopy. The simulations showed a depletion zone of 2Å followed by a layered region of 8Å in the axis perpendicular to the hydrophobic surface.

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.

Molecular features of hydration layers probed by atomic force microscopy

2018 ◽  
Vol 20 (48) ◽  
pp. 30492-30501 ◽  
Author(s):  
Zhengqing Zhang ◽  
Seol Ryu ◽  
Yoonho Ahn ◽  
Joonkyung Jang
Keyword(s):  
Atomic Force Microscopy ◽  
Molecular Dynamic ◽  
Molecular Dynamic Simulations ◽  
Dynamic Simulations ◽  
Force Microscopy ◽  
Molecular Features ◽  
Atomic Force ◽  
Hydration Layers

The molecular features of the hydration layers probed by a nanoscale tip were uncovered by using molecular dynamic simulations.

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

Self-organization of phthalocyanines on Al2O3 (1120) in aligned and ordered films

2004 ◽  
Vol 19 (7) ◽  
pp. 2061-2067 ◽  
Author(s):  
E. Barrena ◽  
J.O. Ossó ◽  
F. Schreiber ◽  
M. Garriga ◽  
M.I. Alonso ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Self Organization ◽  
X Ray Diffraction ◽  
Direction Parallel ◽  
Force Microscopy ◽  
Molecular Arrangement ◽  
Atomic Force ◽  
Organization Process ◽  
Microscopy Images ◽  
Molecular Stacking

We studied the self-organization process of F16CuPc films (20–30 ML) on stepped Al2O3 (1120) substrates. X-ray diffraction measurements revealed a highly ordered layered structure with the molecules in a nearly upright configuration. The morphology, investigated by atomic force microscopy, consisted of long (several microns) and narrow (20–100 nm) needlelike terraces unidirectionally aligned along one of the main crystallographic directions of the Al2O3 (1120) surface. High resolution atomic force microscopy images revealed in-plane molecular order with the molecular stacking direction parallel to the needlelike terraces. Such anisotropic morphology is the result of a self-organization process of F16CuPc in elongated crystallites driven to a preferential orientation by the interaction with the substrate. Spectroscopic ellipsometry showed that these films exhibit anisotropic optical properties correlated with the molecular arrangement.

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.

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