New interesting publication by Macrea et. al mentioning the use of NANOSENSORS uniqprobe qp-BioAC:
“Hemostasis requires conversion of fibrinogen to fibrin fibers that generate a characteristic network, interact with blood cells, and initiate tissue repair. The fibrin network is porous and highly permeable, but the spatial arrangement of the external clot face is unknown. Here we show that fibrin transitioned to the blood-air interface through Langmuir film formation, producing a protective film confining clots in human and mouse models. We demonstrated that only fibrin is required for formation of the film, and that it occurred in vitro and in vivo. The fibrin film connected to the underlying clot network through tethering fibers. It was digested by plasmin, and formation of the film was prevented with surfactants. Functionally, the film retained blood cells and protected against penetration by bacterial pathogens in a murine model of dermal infection. Our data show a remarkable aspect of blood clotting in which fibrin forms a protective film covering the external surface of the clot, defending the organism against microbial invasion.”*
The AFM imaging and force measurements mentioned in this article were performed using CB3 of the NANOSENSORS™ uniqprobeqp-BioAC.
*Fraser L. Macrae, Cédric Duval, Praveen Papareddy, Stephen R. Baker, Nadira Yuldasheva, Katherine J. Kearney, Helen R. McPherson, Nathan Asquith, Joke Konings, Alessandro Casini, Jay L. Degen, Simon D. Connell, Helen Philippou, Alisa S. Wolberg, Heiko Herwald, Robert A.S. Ariëns A fibrin biofilm covers blood clots and protects from microbial invasion
Journal of Clinical Investigation. 2018;128(8):3356-3368
The article “A fibrin biofilm covers blood clots and protects from microbial invasion” by Fraser L. Macrae et. al is licensed under the Creative Commons Attribution 4.0 International License. To view a copy of this license, visit http://creativecommons.org/ licenses/by/4.0/.
For this article the AFM images taken with tapping mode in Tris buffer solution were performed with the NANOSENSORS qp-BioAC (cantilever 3, resonance frequency 30kHz).
Yordanka Yordanova, Willem Vanderlinden, Raphael Stoll, Daniel Rüdiger, Andreas Tosstorff, Wolfgang Zaremba, Gerhard Winter, Stefan Zahler & Wolfgang Friess Zn2+-triggered self-assembly of Gonadorelin [6-D-Phe] to produce nanostructures and fibrils
Nature Scientific Reports volume 8, Article number: 11280 (2018)
Please follow this external link to read the full article on the Nature website: https://rdcu.be/4y9J
Abstract: A synthetic derivative, GnRH [6-D-Phe], stable against enzymatic degradation, self-assembles and forms nanostructures and fibrils upon a pH shift in the presence of different concentrations of Zn2+in vitro. Attenuated Total Reflection Fourier Transform Infrared spectroscopy (ATR–FTIR) revealed the existence of higher order assembly of Zn2+: GnRH [6-D-Phe]. Nuclear Magnetic Resonance spectroscopy (NMR) indicated a weak interaction between Zn2+ and GnRH [6-D-Phe]. Atomic Force Microscopy (AFM) showed the existence of GnRH [6-D-Phe] oligomers and fibrils. Molecular Dynamic (MD) simulation of the 10:1 Zn2+: GnRH [6-D-Phe] explored the interaction and dimerization processes. In contrast to already existing short peptide fibrils, GnRH [6-D-Phe] nanostructures and fibrils form in a Tris-buffered pH environment in a controlled manner through a temperature reduction and a pH shift. The lyophilized Zn2+: GnRH [6-D-Phe] assembly was tested as a platform for the sustained delivery of GnRH [6-D-Phe] and incorporated into two different oil vehicle matrices. The in vitro release was slow and continuous over 14 days and not influenced by the oil matrix.