Literature DB >> 23701412

Nanotopographic surfaces with defined surface chemistries from amyloid fibril networks can control cell attachment.

Nicholas P Reynolds1, Katie E Styan, Christopher D Easton, Yali Li, Lynne Waddington, Cecile Lara, John S Forsythe, Raffaele Mezzenga, Patrick G Hartley, Benjamin W Muir.   

Abstract

We show for the first time the possibility of using networks of amyloid fibrils, adsorbed to solid supports and with plasma polymer coatings, for the fabrication of chemically homogeneous surfaces with well-defined nanoscale surface features reminiscent of the topography of the extracellular matrix. The robust nature of the fibrils allows them to withstand the plasma polymer deposition conditions used with no obvious deleterious effect, thus enabling the underlying fibril topography to be replicated at the polymer surface. This effect was seen despite the polymer coating thickness being an order of magnitude greater than the fibril network. The in vitro culture of fibroblast cells on these surfaces resulted in increased attachment and spreading compared to flat plasma polymer films with the same chemical composition. The demonstrated technique allows for the rapid and reproducible fabrication of substrates with nanoscale fibrous topography that we believe will have applications in the development of new biomaterials allowing, for example, the investigation of the effect of extracellular matrix mimicking nanoscale morphology on cellular phenotype.

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Year:  2013        PMID: 23701412     DOI: 10.1021/bm400430t

Source DB:  PubMed          Journal:  Biomacromolecules        ISSN: 1525-7797            Impact factor:   6.988


  8 in total

1.  Cell Adhesion on Amyloid Fibrils Lacking Integrin Recognition Motif.

Authors:  Reeba S Jacob; Edna George; Pradeep K Singh; Shimul Salot; Arunagiri Anoop; Narendra Nath Jha; Shamik Sen; Samir K Maji
Journal:  J Biol Chem       Date:  2016-01-07       Impact factor: 5.157

Review 2.  Molecular interactions of amyloid nanofibrils with biological aggregation modifiers: implications for cytotoxicity mechanisms and biomaterial design.

Authors:  Durga Dharmadana; Nicholas P Reynolds; Charlotte E Conn; Céline Valéry
Journal:  Interface Focus       Date:  2017-06-16       Impact factor: 3.906

Review 3.  Self-assembling peptide and protein amyloids: from structure to tailored function in nanotechnology.

Authors:  Gang Wei; Zhiqiang Su; Nicholas P Reynolds; Paolo Arosio; Ian W Hamley; Ehud Gazit; Raffaele Mezzenga
Journal:  Chem Soc Rev       Date:  2017-07-31       Impact factor: 54.564

Review 4.  Half a century of amyloids: past, present and future.

Authors:  Pu Chun Ke; Ruhong Zhou; Louise C Serpell; Roland Riek; Tuomas P J Knowles; Hilal A Lashuel; Ehud Gazit; Ian W Hamley; Thomas P Davis; Marcus Fändrich; Daniel Erik Otzen; Matthew R Chapman; Christopher M Dobson; David S Eisenberg; Raffaele Mezzenga
Journal:  Chem Soc Rev       Date:  2020-07-07       Impact factor: 54.564

5.  Heparan sulfates facilitate harmless amyloidogenic fibril formation interacting with elastin-like peptides.

Authors:  Federica Boraldi; Pasquale Moscarelli; Brigida Bochicchio; Antonietta Pepe; Anna M Salvi; Daniela Quaglino
Journal:  Sci Rep       Date:  2018-02-15       Impact factor: 4.379

Review 6.  Rational Biological Interface Engineering: Amyloidal Supramolecular Microstructure-Inspired Hydrogel.

Authors:  Qize Xuan; Yibing Wang; Chao Chen; Ping Wang
Journal:  Front Bioeng Biotechnol       Date:  2021-07-19

7.  Characterization of Amyloid Fibril Networks by Atomic Force Microscopy.

Authors:  Mirren Charnley; Jay Gilbert; Owen G Jones; Nicholas P Reynolds
Journal:  Bio Protoc       Date:  2018-02-20

8.  Dairy-Inspired Coatings for Bone Implants from Whey Protein Isolate-Derived Self-Assembled Fibrils.

Authors:  Rebecca Rabe; Ute Hempel; Laurine Martocq; Julia K Keppler; Jenny Aveyard; Timothy E L Douglas
Journal:  Int J Mol Sci       Date:  2020-08-03       Impact factor: 5.923

  8 in total

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