Micromechanical bending of single collagen fibrils using atomic force microscopy

2007 ◽  
Vol 82A (1) ◽  
pp. 160-168 ◽  
Author(s):  
Lanti Yang ◽  
Kees O. van der Werf ◽  
Bart F.J.M. Koopman ◽  
Vinod Subramaniam ◽  
Martin L. Bennink ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Collagen Fibrils ◽  
Force Microscopy ◽  
Atomic Force

scholarly journals Effects of Mitomycin C on Scleral Collagen Fibrils According to Atomic Force Microscopy

2011 ◽  
Vol 52 (6) ◽  
pp. 671
Author(s):  
Hui-Jae Lee ◽  
Samjin Choi ◽  
Youjin Cheong ◽  
Gyeong Bok Jung ◽  
Kyung-Hyun Jin ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Mitomycin C ◽  
Collagen Fibrils ◽  
Force Microscopy ◽  
Atomic Force

scholarly journals High-speed atomic force microscopy reveals strongly polarized movement of clostridial collagenase along collagen fibrils

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Takahiro Watanabe-Nakayama ◽  
Masahiro Itami ◽  
Noriyuki Kodera ◽  
Toshio Ando ◽  
Hiroki Konno
Keyword(s):  
Atomic Force Microscopy ◽  
High Speed ◽  
Collagen Fibrils ◽  
Force Microscopy ◽  
Atomic Force

scholarly journals Cation-Specific Effects on the Self-Assembly of Collagen Molecules Mediated by Acetate on Mica Surface Observed with Atomic Force Microscopy

2017 ◽  
Vol 2017 ◽  
pp. 1-10 ◽  
Author(s):  
Zhiwei Wang ◽  
Qi Xiao ◽  
Xuan Song ◽  
Yunfei Wan ◽  
Jie Zhu
Keyword(s):  
Atomic Force Microscopy ◽  
Self Assembly ◽  
Ionic Concentration ◽  
Collagen Fibrils ◽  
The Self ◽  
Mica Surface ◽  
Force Microscopy ◽  
Specific Effects ◽  
Atomic Force ◽  
Base Method

The well-organized collagen layers on mica surface have drawn extensive attention for its essential applications and studies on the process of self-assembly as a model system. In this work, collagen extracted from fish scales by acid-base method was used to explore the self-assembly characters, and atomic force microscopy was applied to observe the collagen assembled on mica surface mediated by acetate with four different cations, including K+, Na+, Mg2+, and Ca2+. It showed that cations might influence the interaction between collagen fibrils and mica surface at high ionic concentration. And a similar network structure was acquired with uniform pore size for four kinds of acetates; nearly ranged collagen fibrils in the same direction were collected in Mg2+ solutions, while flat films with some fibrils were achieved in K+ solutions. The Hofmeister series and Collins’ model were adapted to explain the effects of cations and acetate on the self-assembly of collagen. These results and analysis would be helpful for directing the pattern of collagen assembly on a solid surface with a potential application in food science and engineering.

Nanomechanical mapping of single collagen fibrils under tension

Nanoscale ◽  
2019 ◽  
Vol 11 (30) ◽  
pp. 14417-14425 ◽  
Author(s):  
Chris J. Peacock ◽  
Laurent Kreplak
Keyword(s):  
Atomic Force Microscopy ◽  
Collagen Fibrils ◽  
Molecular Density ◽  
Force Microscopy ◽  
Atomic Force ◽  
Density Modulation

Atomic force microscopy based nanomechanical mapping reveals that tension alters the nanoscale molecular density modulation along collagen fibrils.

scholarly journals The Subfibrillar Arrangement of Corneal and Scleral Collagen Fibrils as Revealed by Scanning Electron and Atomic Force Microscopy.

2000 ◽  
Vol 63 (2) ◽  
pp. 127-135 ◽  
Author(s):  
Susumu YAMAMOTO ◽  
Hiroya HASHIZUME ◽  
Jiro HITOMI ◽  
Masatsugu SHIGENO ◽  
Shoichi SAWAGUCHI ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Collagen Fibrils ◽  
Force Microscopy ◽  
Atomic Force ◽  
Scanning Electron

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
Sign in / Sign up

Export Citation Format

Share Document