scholarly journals The Inhibitory Effect of Resveratrol on Elastin Amyloidogenesis

2014 ◽  
Vol 2014 ◽  
pp. 1-4
Author(s):  
Antonietta Pepe ◽  
Florian Delaunay ◽  
Angelo Bracalello ◽  
Brigida Bochicchio
Keyword(s):  
Molecular Structure ◽  
Atomic Force Microscopy ◽  
Self Assembly ◽  
Inhibitory Effect ◽  
Degenerative Diseases ◽  
Force Microscopy ◽  
Atomic Force ◽  
Circular Dichroïsm

The role of polyphenols in the prevention of degenerative diseases is emerging in the last years. In this report, we will investigate in vitro the inhibitory effect of resveratrol on elastin amyloidogenesis. The effect of resveratrol on molecular structure was investigated by circular dichroism spectroscopy, while the inhibitory effect on self-assembly was evaluated by turbidimetry as a function of temperature and by atomic force microscopy.

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.

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

The role of cross-linking in the scratch resistance of organic coatings: An investigation using Atomic Force Microscopy

Wear ◽  
2019 ◽  
Vol 418-419 ◽  
pp. 151-159 ◽  
Author(s):  
Juan F. Gonzalez-Martinez ◽  
Erum Kakar ◽  
Stefan Erkselius ◽  
Nicola Rehnberg ◽  
Javier Sotres
Keyword(s):  
Atomic Force Microscopy ◽  
Scratch Resistance ◽  
Organic Coatings ◽  
Cross Linking ◽  
Force Microscopy ◽  
Atomic Force

scholarly journals Nanostructural and mechanical changes in the sclera following proteoglycan depletion

2018 ◽  
Vol 2 (2) ◽  
pp. 14-17
Author(s):  
Zhuola Zhuola ◽  
Steve Barrett ◽  
Yalda Ashraf Kharaz ◽  
Riaz Akhtar
Keyword(s):  
Mechanical Properties ◽  
Collagen Fibril ◽  
Enzymatic Degradation ◽  
Ocular Tissues ◽  
Force Microscopy ◽  
Nanomechanical Properties ◽  
Atomic Force ◽  
Fibril Morphology

The mechanical properties of ocular tissues, such as the sclera, have a major impact on healthy eye function, and are governed by the properties and composition of the microstructural components. For example, biomechanical degradation associated with myopia occurs alongside a reduction of proteoglycans (PGs). In this study, the role of PG degradation in the nanomechanical properties of the porcine sclera is explored. In-vitro enzymatic degradation of PGs was conducted with α-amylase and chondroitinase ABC enzymes. Collagen fibril morphology and nanomechanical stiffness were measured with atomic force microscopy (AFM). The elastic modulus of the tissue was reduced in all enzyme-treated samples relative to controls. In addition, collagen fibril organization was disrupted by PG depletion. Our data demonstrate that PGs play an important role in determining not only the mechanical properties at these length scales, but also collagen fibril arrangement.

scholarly journals Visualization by atomic force microscopy of tobacco mosaic virus movement protein–RNA complexes formed in vitro

2001 ◽  
Vol 82 (6) ◽  
pp. 1503-1508 ◽  
Author(s):  
O. I. Kiselyova ◽  
I. V. Yaminsky ◽  
E. M. Karger ◽  
O. Yu. Frolova ◽  
Y. L. Dorokhov ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Movement Protein ◽  
Structural Conversion ◽  
Force Microscopy ◽  
Rna Transcripts ◽  
Atomic Force ◽  
Rna Complexes

The structure of complexes formed in vitro by tobacco mosaic virus (TMV)-coded movement protein (MP) with TMV RNA and short (890 nt) synthetic RNA transcripts was visualized by atomic force microscopy on a mica surface. MP molecules were found to be distributed along the chain of RNA and the structure of MP–RNA complexes depended on the molar MP:RNA ratios at which the complexes were formed. A rise in the molar MP:TMV RNA ratio from 20:1 to 60–100:1 resulted in an increase in the density of the MP packaging on TMV RNA and structural conversion of complexes from RNase-sensitive ‘beads-on-a-string’ into a ‘thick string’ form that was partly resistant to RNase. The ‘thick string’-type RNase-resistant complexes were also produced by short synthetic RNA transcripts at different MP:RNA ratios. The ‘thick string’ complexes are suggested to represent clusters of MP molecules cooperatively bound to discrete regions of TMV RNA and separated by protein-free RNA segments.

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