Formation and Topotactical Orientation of Fibrinogen Nanofibrils on Graphite Nanostructures

Reichert, J.; Wei, Gang

doi:10.1002/adem.200900084

Cited by 14 publications

(28 citation statements)

References 48 publications

(65 reference statements)

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“…Single nanofibers as well as networks of fibril‐like structures were found on the hydrophobic PE‐SC crystals. [ 83 ] Interestingly, the fibrous networks resembled the fibrinogen structures previously observed on HOPG nanosteps [ 18 ] although much lower protein concentrations were used. Overall, increasing protein concentrations yielded fibers with larger dimensions and a higher network density: 0.5 µg mL −1 of fibrinogen yielded single nanofibers with an average width of 30 ± 5 nm and 2 µg mL −1 resulted in a nanofiber network with nanofiber widths of 45 ± 10 nm.…”

Section: Fiber Assembly Of Fibrinogen In Vitromentioning

confidence: 79%

“…[ 82 ] Copyright 2018, Elsevier), B) AFM image of single nanofibers on HOPG with nanosteps (reproduced with permission. [ 18 ] Copyright 2009, Wiley‐VCH), C) optical microscope image of nanofiber bundles on poly(methylmethacrylate) surfaces (reproduced with permission. [ 10 ] Copyright 2017, Elsevier), and D) AFM image of nanofiber networks on TOMA clay (reproduced with permission.…”

Section: Fiber Assembly Of Fibrinogen In Vitromentioning

confidence: 99%

“…Jandt and co‐workers even explicitly mentioned the influence of sample drying in their work on HOPG nanosteps where they did not observe any fiber formation during AFM monitoring in liquid. [ 18 ] When fibrinogen solutions are dried during incubation, an increase in protein concentration and ionic strength takes place, which may actually be a major cause for fiber formation. However, this aspect has not been explicitly addressed among the studies available to date.…”

Section: Fiber Assembly Of Fibrinogen In Vitromentioning

confidence: 99%

“…This observation underlines the importance of increasing fibrinogen concentration and ionic strength for fiber assembly, as previously suggested by Jandt and co‐workers. [ 18 ] In another study, which focused on acidic buffer conditions, the Jandt group hypothesized that the presence of positively charged metal ions, such as K + and Na + , can mediate the self‐assembly of fibrinogen molecules into fibers. [ 20 ]…”

Section: Fiber Assembly Of Fibrinogen In Vitromentioning

confidence: 99%

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Principles of Fibrinogen Fiber Assembly In Vitro

Stamboroski

Joshi

Noeske

et al. 2021

Macromolecular Bioscience

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Fibrinogen nanofibers hold great potential for applications in wound healing and personalized regenerative medicine due to their ability to mimic the native blood clot architecture. Although versatile strategies exist to induce fibrillogenesis of fibrinogen in vitro, little is known about the underlying mechanisms and the associated length scales. Therefore, in this manuscript the current state of research on fibrinogen fibrillogenesis in vitro is reviewed. For the first time, the manifold factors leading to the assembly of fibrinogen molecules into fibers are categorized considering three main groups: substrate interactions, denaturing and non‐denaturing buffer conditions. Based on the meta‐analysis in the review it is concluded that the assembly of fibrinogen is driven by several mechanisms across different length scales. In these processes, certain buffer conditions, in particular the presence of salts, play a predominant role during fibrinogen self‐assembly compared to the surface chemistry of the substrate material. Yet, to tailor fibrous fibrinogen scaffolds with defined structure–function‐relationships for future tissue engineering applications, it still needs to be understood which particular role each of these factors plays during fiber assembly. Therefore, the future combination of experimental and simulation studies is proposed to understand the intermolecular interactions of fibrinogen, which induce the assembly of soluble fibrinogen into solid fibers.

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Section: Fiber Assembly Of Fibrinogen In Vitromentioning

confidence: 79%

Section: Fiber Assembly Of Fibrinogen In Vitromentioning

confidence: 99%

Section: Fiber Assembly Of Fibrinogen In Vitromentioning

confidence: 99%

Section: Fiber Assembly Of Fibrinogen In Vitromentioning

confidence: 99%

See 2 more Smart Citations

Principles of Fibrinogen Fiber Assembly In Vitro

Stamboroski

Joshi

Noeske

et al. 2021

Macromolecular Bioscience

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“…Fibrinogen has a dimension of ca. 47 × 5 × 5 nm 3 ,32 between the sizes of the two other blood plasma proteins studied by Ganazzoli and Raffaini.…”

Section: Discussionmentioning

confidence: 91%

Fibrinogen Adsorption on Biomaterials – A Numerical Study

Siegismund

Keller

Rettenmayr

2010

Macromolecular Bioscience

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A model for the adsorption of fibrinogen or, in general, non-globular shaped proteins on solid surfaces are presented. Two-dimensional cellular automata simulations of the adsorption of fibrinogen on two different surfaces were performed. The model includes mass transfer toward the surface, adsorption of fibrinogen molecules, and surface diffusion mechanisms for both fibrinogen molecules and clusters. We show that the major physical processes are represented in the recent model. Particularly, the influence of the surface hydrophobicity on the behavior of fibrinogen. Atomic force microscopy images of fibrinogen adsorption on Si model surfaces with different hydrophobicity are compared to the results.

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