Corrosion inhibition by self-assembling nanofilms

2020 ◽  
pp. 107-125
Author(s):  
J. Maria Praveena ◽  
R. Joseph Rathish ◽  
Susai Rajendran ◽  
S. Senthil Kumaran ◽  
Gurmeet Singh ◽  
...  
Keyword(s):  
Corrosion Inhibition ◽  
Self Assembling

Corrosion Inhibition by Self Assembling Monolayers on Carbon Steel

2015 ◽  
Vol 5 (2) ◽  
pp. 113-117
Author(s):  
Somasundaram Gowri ◽  
Jeganathan Sathiyabama ◽  
Susai Rajendran ◽  
Rajendran M. Joany ◽  
Jeyaparkash Jeyasundari ◽  
...  
Keyword(s):  
Carbon Steel ◽  
Corrosion Inhibition ◽  
Self Assembling

Corrosion inhibition of aluminum by oxalate self-assembling monolayer

2019 ◽  
Vol 66 (6) ◽  
pp. 768-773 ◽  
Author(s):  
P. Satyabama ◽  
Susai Rajendran ◽  
Tuan Anh Nguyen
Keyword(s):  
Corrosion Inhibition ◽  
Potentiodynamic Polarization ◽  
Fluorescence Spectra ◽  
Electrochemical Impedance ◽  
Aluminum Surface ◽  
Protective Film ◽  
Content Type ◽  
Self Assembling ◽  
Uv Visible ◽  
Oxalate Ions

Purpose This paper aims to evaluate the inhibition efficiency (IE) of oxalate ions in controlling corrosion of aluminum at pH 10. Design/methodology/approach The IE has been determined by the classical weight loss method. The corrosion behavior of aluminum was investigated by using potentiodynamic polarization and electrochemical impedance measurements. Ultra violet (UV)-visible and Fluorescence spectra have been used to analyze the film formed on the aluminum surface after immersion. Findings The maximum IE was 88 per cent, which was offered by a mixture of 250 ppm oxalate ions and 50 ppm [Zn2+]. Potentiodynamic polarization data revealed that the protective film was formed on the metal surface. UV-visible and Fluorescence spectra indicated the presence of Al3+−oxalate complex in the protective film formed on aluminum substrate after immersion in [OX]/[Zn2+] solution. Originality/value The findings of this work shed more light on the corrosion inhibition of aluminum by oxalate self-assembling monolayers.

Torus Circumference and Thickness Parameters From a Linear DNA Size Series Suggest How Toruses Self-Assemble

1985 ◽  
Vol 43 ◽  
pp. 522-523
Author(s):  
George C. Ruben ◽  
Kenneth A. Marx
Keyword(s):  
Tertiary Structure ◽  
Dna Complexes ◽  
Tertiary Structures ◽  
Self Assembling ◽  
Double Stranded Dna ◽  
Calf Thymus ◽  
Dna Organization ◽  
Condensed Dna ◽  
Dna Size

Certain double stranded DNA bacteriophage and viruses are thought to have their DNA organized into large torus shaped structures. Morphologically, these poorly understood biological DNA tertiary structures resemble spermidine-condensed DNA complexes formed in vitro in the total absence of other macromolecules normally synthesized by the pathogens for the purpose of their own DNA packaging. Therefore, we have studied the tertiary structure of these self-assembling torus shaped spermidine- DNA complexes in a series of reports. Using freeze-etch, low Pt-C metal (10-15Å) replicas, we have visualized the microscopic DNA organization of both calf Thymus( CT) and linear 0X-174 RFII DNA toruses. In these structures DNA is circumferentially wound, continuously, around the torus into a semi-crystalline, hexagonal packed array of parallel DNA helix sections.

Structure–property studies of self-assembling [n.n]paracyclophanes

2020 ◽  
Author(s):  
Will R Henderson ◽  
Danielle E. Fagnani ◽  
Yu Zhu ◽  
Guancen Liu ◽  
Ronald K. Castellano
Keyword(s):  
Structure Property ◽  
Self Assembling

Self assembling mirrors

Nature ◽  
1999 ◽  
Author(s):  
Philip Ball
Keyword(s):  
Self Assembling

Combinatorial Peptide Libraries for Selecting Inorganic-Binding Proteins: A Step in Molecular Biomimetics

2003 ◽  
Vol 773 ◽  
Author(s):  
C. Tamerler ◽  
S. Dinçer ◽  
D. Heidel ◽  
N. Karagûler ◽  
M. Sarikaya
Keyword(s):  
Binding Proteins ◽  
Building Blocks ◽  
Molecular Engineering ◽  
Inorganic Materials ◽  
Combinatorial Peptide Libraries ◽  
Self Assembling ◽  
Complex Functions ◽  
Recent Developments ◽  
Specific Proteins ◽  
Molecular Biomimetics

AbstractProteins, one of the building blocks in organisms, not only control the assembly in biological systems but also provide most of their complex functions. It may be possible to assemble materials for practical technological applications utilizing the unique advantages provided by proteins. Here we discuss molecular biomimetic pathways in the quest for imitating biology at the molecular scale via protein engineering. We use combinatorial biology protocols to select short polypeptides that have affinity to inorganic materials and use them in assembling novel hybrid materials. We give an overview of some of the recent developments of molecular engineering towards this goal. Inorganic surface specific proteins were identified by using cell surface and phage display technologies. Examples of metal and metal oxide specific polypeptides were represented with an emphasis on certain level of specificities. The recognition and self assembling characteristics of these inorganic-binding proteins would be employed in develeopment of hybrid multifunctional materials for novel bio- and nano-technological applications.

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