scholarly journals Loading efficiency of doxorubicin into the micelle-like structures formed by function-spacer-lipid constructs self-assembly depends on constructs’ functional part

2021 ◽  
Vol 2058 (1) ◽  
pp. 012003
Author(s):  
A R Tarasova ◽  
I S Vaskan ◽  
A V Zalygin ◽  
P S Troitskaya ◽  
N V Bovin ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Structural Properties ◽  
Self Assembly ◽  
Potential Drug ◽  
Supramolecular Systems ◽  
Force Microscopy ◽  
Atomic Force ◽  
Loading Efficiency ◽  
Functional Part ◽  
Drug Nanocarriers

Abstract Supramolecular self-assemble systems based on neoglycolipids: Galili-Ad-CMG2-Ad-DOPE, A(type2)-Ad-CMG2-Ad-DOPE are studied here and compared with the well-studied Biotin-CMG2-Ad-DOPE, as well as with their combinations with NH2-CMG2-Ad-DOPE. They are function-spacer-lipid constructs with unique structure that allows them to form micelle-like supramers and be stable, what makes them a potential drug nanocarriers. The structural properties of the obtained supramolecular systems are studied depending on their functional part, and the loading efficiency of doxorubicin into the supramers is determined to reveal the influence of the functional part. The resulting supramers were separated from the unbound molecules by dialysis, the nanoparticles morphology were studied by atomic force microscopy, and the loading efficiency was calculated based on spectrophotometry data. The encapsulation of doxorubicin was confirmed based on changes in the size and shape of the supramers, as well as a decrease in the ratio of unbound molecules. According to the loading efficiency calculations, it was estimated that supramers formed by A(type2)-Ad-CMG2-Ad-DOPE are the most efficient nanocarriers with loading efficiency of 82 %. Supramers formed by NH2-CMG2-Ad-DOPE (no functional part) showed 1.5 times less efficiency. Finally, the least efficient carriers are supramers formed by Biotin-CMG2-Ad-DOPE (14%).

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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