Interactions of human von Willebrand Factor with a hydrophobic self-assembled monolayer studied by atomic force microscopy

1994 ◽  
Vol 28 (9) ◽  
pp. 971-980 ◽  
Author(s):  
Christopher A. Siedlecki ◽  
Steven J. Eppell ◽  
Roger E. Marchant
Keyword(s):  
Atomic Force Microscopy ◽  
Von Willebrand Factor ◽  
Self Assembled Monolayer ◽  
Force Microscopy ◽  
Atomic Force ◽  
Self Assembled ◽  
Von Willebrand ◽  
Willebrand Factor

Shear and Substrate Dependent Changes in Fibrinogen and Von Willebrand Factor Studied by Atomic Force Microscopy

1998 ◽  
Vol 4 (S2) ◽  
pp. 924-925
Author(s):  
Roger E. Marchant ◽  
P. Sidney Sit ◽  
Madhusudan Raghavachari ◽  
Christopher A. Siedlecki
Keyword(s):  
Atomic Force Microscopy ◽  
Von Willebrand Factor ◽  
Hydrophobic Surface ◽  
Three Dimensions ◽  
Human Fibrinogen ◽  
Force Microscopy ◽  
Atomic Force ◽  
Aqueous Conditions ◽  
Von Willebrand ◽  
Willebrand Factor

Atomic force microscopy (AFM) provides unique opportunities to study cell-surface and molecular scale interactions in three dimensions under aqueous conditions. Two plasma proteins, von Willebrand Factor (vWf) and fibrinogen, play central roles in the regulation of hemostasis and thrombosis by participating in coagulation and facilitating adhesion and aggregation of activated platelets. vWf and fibrinogen are believed to facilitate platelet adhesion under regions of relatively high and low vascular wall shear stress, respectively. Consequently, elucidating vWf and fibrinogen structure-function relations under shear is of considerable importance in developing a comprehensive understanding of the pathophysiology of thrombogenesis. Previously, we reported on molecular level AFM images of human vWf during shear-induced structural transition and human fibrinogen under aqueous conditions when both proteins were adsorbed on a hydrophobic surface. This presentation will report on the shear dependent interactions of dimeric and multimeric vWf with a hydrophobic surface and the substrate-dependent interactions of fibrinogen.

scholarly journals Interactions of von Willebrand factor on mica studied by atomic force microscopy

1992 ◽  
Vol 148 (1) ◽  
pp. 261-272 ◽  
Author(s):  
Roger E Marchant ◽  
A.Scott Lea ◽  
Joseph D Andrade ◽  
Paula Bockenstedt
Keyword(s):  
Atomic Force Microscopy ◽  
Von Willebrand Factor ◽  
Force Microscopy ◽  
Atomic Force ◽  
Von Willebrand ◽  
Willebrand Factor

Comparison of plasma-derived and recombinant von Willebrand factor by atomic force microscopy

2010 ◽  
Vol 104 (09) ◽  
pp. 523-530 ◽  
Author(s):  
Birgit Seyfried ◽  
Gernot Friedbacher ◽  
Hanspeter Rottensteiner ◽  
Hans Peter Schwarz ◽  
Hartmut Ehrlich ◽  
...  
Keyword(s):  
Atomic Force Microscopy ◽  
Shear Stress ◽  
Von Willebrand Factor ◽  
Globular Domain ◽  
Force Microscopy ◽  
Molecular Weights ◽  
Atomic Force ◽  
Similar Range ◽  
Von Willebrand ◽  
Willebrand Factor

SummaryHuman plasma protein von Willebrand factor (VWF) is composed of a series of multimers with molecular weights ranging from 600 to 20,000 kDa or even more. Plasma-derived VWF (pdVWF) and recombinant VWF (rVWF) differ in that the ultra-large molecular weight multimer portion present in rVWF is usually missing in pdVWF due to partial cleavage of VWF by the plasma protease ADAMTS13. Here, tapping mode atomic force microscopy (TM-AFM) was used to visualise the shape and size of rVWF and pdVWF. The morphology of the variants of VWF was comparable, containing both globular and stretched domains. Mean chain lengths of the filaments and diameters of the core globular domains were determined and analysed on a statistical basis. About 72% of the pdVWF molecules and 70% of the rVWF molecules were 100–300 nm long. The portion of very long molecules (>300 nm) was only slightly greater in rVWF than in pdVWF (20% vs. 18%). The diameters of the globular core structures were in the range of 12 to 30 nm for both types of VWF. Inspection of a purified rVWF dimer revealed a similar range for the globular domain (14–32 nm). Finally, we demonstrate a dramatic conformational change for rVWF upon exposure to high shear stress, as has been reported for pdVWF. Our TM-AFM data show that the overall structure of rVWF is similar to that of pdVWF and that rVWF will extend its conformation under shear stress, which is required to exert its function in primary haemostasis.

Comparative Study of Field Emission-Scanning Electron Microscopy and Atomic Force Microscopy to Assess Self-assembled Monolayer Coverage on Any Type of Substrate

1999 ◽  
Vol 5 (6) ◽  
pp. 413-419 ◽  
Author(s):  
Bernardo R.A. Neves ◽  
Michael E. Salmon ◽  
Phillip E. Russell ◽  
E. Barry Troughton
Keyword(s):  
Electron Microscopy ◽  
Scanning Electron Microscopy ◽  
Atomic Force Microscopy ◽  
Comparative Study ◽  
Field Emission ◽  
Self Assembled Monolayer ◽  
Force Microscopy ◽  
Atomic Force ◽  
Self Assembled ◽  
Scanning Electron

Abstract: In this work, we show how field emission–scanning electron microscopy (FE-SEM) can be a useful tool for the study of self-assembled monolayer systems. We have carried out a comparative study using FE-SEM and atomic force microscopy (AFM) to assess the morphology and coverage of self-assembled monolayers (SAM) on different substrates. The results show that FE-SEM images present the same qualitative information obtained by AFM images when the SAM is deposited on a smooth substrate (e.g., mica). Further experiments with rough substrates (e.g., Al grains on glass) show that FE-SEM is capable of unambiguously identifying SAMs on any type of substrate, whereas AFM has significant difficulties in identifying SAMs on rough surfaces.

Adhesion and Friction at Graphene/Self-Assembled Monolayer Interfaces Investigated by Atomic Force Microscopy

2017 ◽  
Vol 121 (10) ◽  
pp. 5635-5641 ◽  
Author(s):  
Meagan B. Elinski ◽  
Benjamin D. Menard ◽  
Zhuotong Liu ◽  
James D. Batteas
Keyword(s):  
Atomic Force Microscopy ◽  
Self Assembled Monolayer ◽  
Force Microscopy ◽  
Atomic Force ◽  
Self Assembled
Sign in / Sign up

Export Citation Format

Share Document