Nanoscale characterization of oral streptococci early-adhesion to crosslinked type-I collagen matrices by atomic force microscopy

2021 ◽  
Author(s):  
Sebastian Aguayo
Keyword(s):  
Atomic Force Microscopy ◽  
Type I Collagen ◽  
Type I ◽  
Oral Streptococci ◽  
Collagen Matrices ◽  
Force Microscopy ◽  
Atomic Force ◽  
Nanoscale Characterization

scholarly journals Recent Applications of Advanced Atomic Force Microscopy in Polymer Science: A Review

Polymers ◽  
2020 ◽  
Vol 12 (5) ◽  
pp. 1142 ◽  
Author(s):  
Phuong Nguyen-Tri ◽  
Payman Ghassemi ◽  
Pascal Carriere ◽  
Sonil Nanda ◽  
Aymen Amine Assadi ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Chemical Characterization ◽  
Super Resolution ◽  
Polymeric Materials ◽  
Polymer Materials ◽  
Polymer Science ◽  
Force Microscopy ◽  
Atomic Force ◽  
Nanoscale Characterization

Atomic force microscopy (AFM) has been extensively used for the nanoscale characterization of polymeric materials. The coupling of AFM with infrared spectroscope (AFM-IR) provides another advantage to the chemical analyses and thus helps to shed light upon the study of polymers. This paper reviews some recent progress in the application of AFM and AFM-IR in polymer science. We describe the principle of AFM-IR and the recent improvements to enhance its resolution. We also discuss the latest progress in the use of AFM-IR as a super-resolution correlated scanned-probe infrared spectroscopy for the chemical characterization of polymer materials dealing with polymer composites, polymer blends, multilayers, and biopolymers. To highlight the advantages of AFM-IR, we report several results in studying the crystallization of both miscible and immiscible blends as well as polymer aging. Finally, we demonstrate how this novel technique can be used to determine phase separation, spherulitic structure, and crystallization mechanisms at nanoscales, which has never been achieved before. The review also discusses future trends in the use of AFM-IR in polymer materials, especially in polymer thin film investigation.

Shape and size of epididymal sperm from Gir bulls using atomic force microscopy: A nanoscale characterization of epididymal sperm

2020 ◽  
Vol 20 (1) ◽  
pp. 37-41
Author(s):  
Andrielle Thainar Mendes Cunha ◽  
Luciano Paulino Silva ◽  
José Oliveira Carvalho ◽  
Margot Alves Nunes Dode
Keyword(s):  
Atomic Force Microscopy ◽  
Epididymal Sperm ◽  
Force Microscopy ◽  
Atomic Force ◽  
Nanoscale Characterization ◽  
Shape And Size

scholarly journals Nanoscale characterization of squaraine-fullerene-based photovoltaic active layers by atomic force microscopy mechanical and electrical property mapping

2019 ◽  
Vol 669 ◽  
pp. 120-132 ◽  
Author(s):  
Tonya Coffey ◽  
Andrew Seredinski ◽  
Jake N. Poler ◽  
Crystal Patteson ◽  
William H. Watts ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Electrical Property ◽  
Force Microscopy ◽  
Active Layers ◽  
Atomic Force ◽  
Nanoscale Characterization

scholarly journals Influence of Matrix Metalloprotease on the Flexibility of Type I Collagen Fibrils Studied By Atomic Force Microscopy

2010 ◽  
Vol 98 (3) ◽  
pp. 29a
Author(s):  
Arkady Bitler ◽  
Emanuel Perugia ◽  
Inna Solomonov ◽  
Robert Visse ◽  
Joseph Orgel ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Type I Collagen ◽  
Collagen Fibrils ◽  
Type I ◽  
Matrix Metalloprotease ◽  
Force Microscopy ◽  
Atomic Force

scholarly journals Atomic Force Microscopy for Collagen-Based Nanobiomaterials

2017 ◽  
Vol 2017 ◽  
pp. 1-14 ◽  
Author(s):  
Andreas Stylianou
Keyword(s):  
Thin Films ◽  
Atomic Force Microscopy ◽  
Collagen Type I ◽  
Quantitative Information ◽  
Fibrillar Structure ◽  
Type I ◽  
Force Microscopy ◽  
Atomic Force ◽  
Wide Range

Novel nanobiomaterials are increasingly gaining ground in bioengineering research. Among the numerous biomaterials, collagen-nanobiomaterials, such as collagen thin films, are of great interest since they present a wide range of applications in the fields of biomaterials, tissue engineering, and biomedicine. Collagen type I is the most abundant protein within extracellular matrix and, due to its unique characteristics, is widely used as biomaterial. A thorough characterization of the structure and properties of nanomaterials can be achieved by Atomic Force Microscopy (AFM). AFM is a very powerful tool which can be used to obtain qualitative or quantitative information without destroying the collagen fibrillar structure. This mini review covers issues related to the use of AFM for studying the structure and mechanical properties of collagen-based nanobiomaterials, collagen-substrate interactions during the formation of collagen thin films, collagen-cells interactions, and the collagen-optical radiation interactions.

scholarly journals Nanoscale characterization of all-oxide core-shell nanorod heterojunction using intermodulation atomic force microscopy (AFM) methods

2021 ◽  
Author(s):  
Illia Dobryden ◽  
Riccardo Borgani ◽  
Federica Rigoni ◽  
Pedram Ghamgosar ◽  
Isabella Concina ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Electrical Properties ◽  
Contact Potential Difference ◽  
Core Shell ◽  
Contact Potential ◽  
Distribution Maps ◽  
Force Microscopy ◽  
Atomic Force ◽  
Nanoscale Characterization

The electrical properties of an all-oxide core-shell ZnO-Co3O4 nanorod heterojunction were studied in dark and under UV-vis illumination. The contact potential difference and current distribution maps were obtained utilizing new...

MORPHOLOGY OF ADSORBED COLLAGEN LAYERS OBSERVED BY ATOMIC FORCE MICROSCOPY

2009 ◽  
Vol 21 (05) ◽  
pp. 311-316
Author(s):  
Yih-Pey Yang ◽  
Chia-Chi Lin
Keyword(s):  
Atomic Force Microscopy ◽  
Type I Collagen ◽  
Fibrillar Structure ◽  
Collagen Molecule ◽  
Nanometer Scale ◽  
Type I ◽  
Force Microscopy ◽  
Atomic Force

The interaction between cells and biomaterials strongly depends on the assembled structure of collagen adsorption upon the solid surface. Due to its self-assembling property, Type I collagen may aggregate and form fibrils in vivo and in vitro. This study utilizes an atomic force microscope to investigate nanometer-scale organization of adsorbed Type I collagen layers on mica and on poly(methyl methacrylate) (PMMA). We have observed various film morphologies, depending on substrate hydrophobicity and the state of collagen solution used. On mica, the atomic force microscopy (AFM) study obtains dense felt-like structures of randomly distributed assemblies. Images of network-like assemblies composed of interwoven fibrils appear on PMMA. According to the above results, we believe that these assemblies are associated at the interface rather than aggregated in the solution. This work also investigates the adsorbed collagen structure on PMMA after collagen aggregation in solution, to realize the relation between adsorption and aggregation. Consequently, the result exhibits a dendritic fibrillar structure adsorbed on PMMA, following collagen molecule aggregation, to form a fibrillar structure in the solution. This result suggests that the adsorption of aggregates preformed in the solution is preferable to collagen molecules adsorption. This research created all assembled structures of adsorbed collagen layers in nanometer-scale thickness.

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