scholarly journals Self-organization of amino-acid-derived NDI assemblies into a nanofibrillar superstructure with humidity sensitive n-type semiconducting properties

2017 ◽  
Vol 53 (70) ◽  
pp. 9713-9716 ◽  
Author(s):  
Marco A. Squillaci ◽  
Grzegorz Markiewicz ◽  
Anna Walczak ◽  
Artur Ciesielski ◽  
Artur R. Stefankiewicz ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Amino Acid ◽  
Solid State ◽  
Nmr Spectroscopy ◽  
Self Assembly ◽  
Self Organization ◽  
Force Microscopy ◽  
Atomic Force ◽  
Semiconducting Properties

The hierarchical self-assembly of l-tyrosine substituted naphthalenediimide has been explored in solution by NMR spectroscopy and in the solid-state by atomic force microscopy.

Atomic force microscopy study of self-organization of chiral azobenzene derived from amino acid

2003 ◽  
Vol 220 (1-4) ◽  
pp. 224-230 ◽  
Author(s):  
Yanjie Zhang ◽  
Changhui Tan ◽  
Qingsheng Liu ◽  
Ran Lu ◽  
Yanlin Song ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Amino Acid ◽  
Microscopy Study ◽  
Self Organization ◽  
Atomic Force Microscopy Study ◽  
Force Microscopy ◽  
Atomic Force

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 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.

Solid-State DNA Sizing by Atomic Force Microscopy

1998 ◽  
Vol 70 (10) ◽  
pp. 2123-2129 ◽  
Author(s):  
Ye Fang ◽  
Thomas S. Spisz ◽  
Tim Wiltshire ◽  
Neill P. D'Costa ◽  
Isaac N. Bankman ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Solid State ◽  
Force Microscopy ◽  
Atomic Force

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.

Sign in / Sign up

Export Citation Format

Share Document