Bioselectivity of silk protein-based materials and their bio-inspired applications

• Hendrik Bargel,
• Vanessa T. Trossmann,
• Christoph Sommer and
• Thomas Scheibel

Beilstein J. Nanotechnol. 2022, 13, 902–921, doi:10.3762/bjnano.13.81

• fibronectin, fibrinogen, vitronectin, and complement component iC3b [13]. Divalent cations, such as Mg2+ and Ca2+, are involved in ligand binding. Individual integrins can bind more than one ligand, and vice versa. However, the cellular environment may influence ligand specificity within a particular cell

• collagens, laminins, fibronectin, and elastin, which contain several short peptide recognition and binding motifs in their amino acid sequence for interaction with specific cellular surface integrins or other types of receptors [23]. Within the ECM, fibronectin is the best-known attachment site for cells by

• interacting with members of the integrin family of cell surface proteins. However, fibronectin is a multifunctional adhesion molecule, also binding to other protein constituents of the ECM such as fibrin, collagen, and heparin [24]. Thus, fibronectin is involved in several physiological events such as

Gelatin nanoparticles with tunable mechanical properties: effect of crosslinking time and loading

• Agnes-Valencia Weiss,
• Daniel Schorr,
• Julia K. Metz,
• Metin Yildirim,
• Saeed Ahmad Khan and
• Marc Schneider

Beilstein J. Nanotechnol. 2022, 13, 778–787, doi:10.3762/bjnano.13.68

• (10.000 µg/mL), Gibco™, Fisher Scientific, Waltham, MA, USA). All plastic devices used for hAELVi culture were precoated with a 1% v/v fibronectin (Corning, NY, USA)–collagen (Sigma-Aldrich, Darmstadt, Germany) solution. Methods Preparation of gelatin nanoparticles The preparation was based on the

Micro- and nanotechnology in biomedical engineering for cartilage tissue regeneration in osteoarthritis

• Zahra Nabizadeh,
• Mahmoud Nasrollahzadeh,
• Hamed Daemi,
• Mohamadreza Baghaban Eslaminejad,
• Ali Akbar Shabani,
• Mehdi Dadashpour,
• Majid Mirmohammadkhani and
• Davood Nasrabadi

Beilstein J. Nanotechnol. 2022, 13, 363–389, doi:10.3762/bjnano.13.31

• traditionally incorporated in scaffolds to provide proper cell–matrix interactions for tissue regeneration [149]. Among these, cell adhesion motifs including RGD peptide and fibronectin fragments at the nanoscale are widely used to enhance the cell motility and adhesion functionality of hydrogels [178]. For

Engineered titania nanomaterials in advanced clinical applications

• Padmavati Sahare,
• Paulina Govea Alvarez,
• Juan Manual Sanchez Yanez,
• Gabriel Luna-Bárcenas,
• Samik Chakraborty,
• Sujay Paul and
• Miriam Estevez

Beilstein J. Nanotechnol. 2022, 13, 201–218, doi:10.3762/bjnano.13.15

• affinities for the nanoparticle surface or the corona. Recently, Zhongru Gou et al. investigated the amount and type of cell adhesion-related proteins (such as fibronectin, vitronectin, and laminin) from serum adsorbed on titanium nanotube arrays. Their findings suggest that all the abovementioned proteins

Cardiomyocyte uptake mechanism of a hydroxyapatite nanoparticle mediated gene delivery system

• Hiroaki Komuro,
• Masahiro Yamazoe,
• Kosuke Nozaki,
• Akiko Nagai and
• Tetsuo Sasano

Beilstein J. Nanotechnol. 2020, 11, 1685–1692, doi:10.3762/bjnano.11.150

• 25 μg/mL fibronectin solution (Wako) prepared in a 0.02% gelatin solution (Wako) in order to increase cell adhesion. The cells were grown in a humidified incubator at 37 °C containing 5% CO2. Cytotoxicity assay The cytotoxicity of HAp/pDNA complexes or endocytosis inhibitors was verified by an MTT

Applications of superparamagnetic iron oxide nanoparticles in drug and therapeutic delivery, and biotechnological advancements

• Maria Suciu,
• Corina M. Ionescu,
• Alexandra Ciorita,
• Septimiu C. Tripon,
• Dragos Nica,
• Hani Al-Salami and
• Lucian Barbu-Tudoran

Beilstein J. Nanotechnol. 2020, 11, 1092–1109, doi:10.3762/bjnano.11.94

• histidine–proline-rich glycoprotein, kininogen, prekallikrein, mannose-binding lectins, complement factors, clotting factors, immunoglobulins, fibronectin, and fibrinogen. They obtained the equivalent of 1 mg of proteins bound to 1 mg of iron oxide (in the case of extensive washing). This corona of proteins

Identification of physicochemical properties that modulate nanoparticle aggregation in blood

• Ludovica Soddu,
• Duong N. Trinh,
• Eimear Dunne,
• Dermot Kenny,
• Giorgia Bernardini,
• Ida Kokalari,
• Arianna Marucco,
• Marco P. Monopoli and
• Ivana Fenoglio

Beilstein J. Nanotechnol. 2020, 11, 550–567, doi:10.3762/bjnano.11.44

• without forming stable adhesions. After infringement of the vasculature proteins like VWF, collagen and fibronectin are exposed on the sub-endothelial matrix and act as ligands for the platelet surface receptors, such as glycoproteins like GPVI and GPIbα, that lead the platelet adhesion to the affected

• mobilize intracellular Ca2+, which instigates platelet shape change, degranulation, and up-regulation of the adhesive function of another platelet surface receptor, integrin αIIbβ3 [35]. The active conformation of αIIbβ3 integrin can then bind fibrinogen, VWF and fibronectin with high affinity, allowing

Evaluation of quantum dot conjugated antibodies for immunofluorescent labelling of cellular targets

• Jennifer E. Francis,
• David Mason and
• Raphaël Lévy

Beilstein J. Nanotechnol. 2017, 8, 1238–1249, doi:10.3762/bjnano.8.125

• -Ab. A Qdot 625-Ab concentration of 20 nM was used, as it has been shown that a high concentration of Qdot-Abs improves specific labelling and signal-to-noise ratio [21]. Initially, to assess the labelling efficiency of Qdot-Abs, the extracellular matrix (ECM) protein fibronectin was dual labelled

• with Qdot 625-Ab and Dye-Ab (Alexa Fluor 488). Fibronectin is abundant at the cell surface and therefore, would not be expected to display any artifacts associated with accessibility. Indeed, in this case similar labelling was achieved with Qdot 625 and Alexa Fluor 488 (Figure 2). Labelling of

• primary antibody was also prepared, showing negligible unspecific binding of Alexa Fluor 488 and Qdot 625 to HeLa cells (Figure S4 in Supporting Information File 1). Labelling intracellular complexes: Both fibronectin and β-tubulin are highly abundant proteins. Furthermore, their antigens are relatively

Uptake of the proteins HTRA1 and HTRA2 by cells mediated by calcium phosphate nanoparticles

• Olga Rotan,
• Katharina N. Severin,
• Simon Pöpsel,
• Alexander Peetsch,
• Melisa Merdanovic,
• Michael Ehrmann and
• Matthias Epple

Beilstein J. Nanotechnol. 2017, 8, 381–393, doi:10.3762/bjnano.8.40

• cells and a decreased tumour growth have been observed upon HTRA1 overexpression [33][34]. A wide range of extracellular matrix proteins has been reported as substrates of the protease HTRA1. Among them are fibronectin, decorin, fibromodulin, aggrecan, type ii collagen, biglycan, clusterin, ADAM9

Nano- and microstructured materials for in vitro studies of the physiology of vascular cells

• Alexandra M. Greiner,
• Adria Sales,
• Hao Chen,
• Sarah A. Biela,
• Dieter Kaufmann and
• Ralf Kemkemer

Beilstein J. Nanotechnol. 2016, 7, 1620–1641, doi:10.3762/bjnano.7.155

• obtain nanofibers from natural proteins such as fibronectin. Recently, an alternative method has been developed where nanofibers of extruded fibronectin through a nanoporous aluminum oxide membrane were obtained. This method is based on a mechanical force to provoke fibrillogenesis (generation of fibers

• ) of fibronectin [78]. Nanoskiving is a less conventional technique for the fabrication of nanostructures, where basically a thin metal film is embedded between two epoxy layers. One of the epoxy layers contains a nano- or micropattern on which the metal layer is deposited (e.g., through vapor

• as fibronectin, laminin, collagen and vitronectin [151][152][153][154]. One has to keep in mind, that in most in vitro and particularly in in vivo environments plenty of different proteins are getting in contact with the surface and alter the initial coating, thus making it difficult to maintain

Advanced atomic force microscopy techniques III

• Thilo Glatzel and
• Thomas Schimmel

Beilstein J. Nanotechnol. 2016, 7, 1052–1054, doi:10.3762/bjnano.7.98

• interaction in liquid media [28]. A software package, dForce, was also presented that allows for a better understanding of amplitude modulation and bimodal AFM experiments in air or liquid [29]. A method for the calibration of the torsional force by using human fibronectin and its monoclonal antibody was

Active multi-point microrheology of cytoskeletal networks

• Tobias Paust,
• Tobias Neckernuss,
• Lina Katinka Mertens,
• Ines Martin,
• Michael Beil,
• Paul Walther,
• Thomas Schimmel and
• Othmar Marti

Beilstein J. Nanotechnol. 2016, 7, 484–491, doi:10.3762/bjnano.7.42

• particles embedded in a matrix is correlated [11][12]. There, it was shown for fibronectin that this correlation leads to calculated viscoelastic parameters in good agreement with classical rheology. Actin networks exhibit a similar correlated movement [13]. It was shown that the single-particle and the

Probing fibronectin–antibody interactions using AFM force spectroscopy and lateral force microscopy

• Andrzej J. Kulik,
• Małgorzata Lekka,
• Kyumin Lee,
• Grazyna Pyka-Fościak and
• Wieslaw Nowak

Beilstein J. Nanotechnol. 2015, 6, 1164–1175, doi:10.3762/bjnano.6.118

• quantitative results requires the complex and tedious calibration of a torsional force. Here, a new and relatively simple method for the calibration of the torsional force is presented. The proposed calibration method is validated through the measurement of the interaction forces between human fibronectin and

• : fibronectin; lateral force microscopy; molecular recognition; torsional forces calibration; Introduction The invention of atomic force microscopy (AFM) opened up new areas of research as it can probe various biological structures with nanometer resolution, including images of DNA [1], proteins [2], and

• molecular interactions, we have measured interaction forces between protein fibronectin (FN) and monoclonal antibody against FN (FN-Mab) using both AFM-FS and LFM techniques. The relation between the unbinding force and the loading rate obtained by AFM-FS was compared with the corresponding relation

Pulmonary surfactant augments cytotoxicity of silica nanoparticles: Studies on an in vitro air–blood barrier model

• Jennifer Y. Kasper,
• Lisa Feiden,
• Maria I. Hermanns,
• Christoph Bantz,
• Michael Maskos,
• Ronald E. Unger and
• C. James Kirkpatrick

Beilstein J. Nanotechnol. 2015, 6, 517–528, doi:10.3762/bjnano.6.54

• day at a dilution of 1:3 and 1:6 until passage 50 and 35, respectively. Monocultures (MC) in experimental procedures: Prior to seeding cells, the 96-well plates (TPP, Switzerland) or 8 well µ-slides (ibidi) were coated with 50/300 µL fibronectin for 1 h at 37 °C (5 µg/mL, Roche Diagnostics, Mannheim

Increasing throughput of AFM-based single cell adhesion measurements through multisubstrate surfaces

• Miao Yu,
• Nico Strohmeyer,
• Jinghe Wang,
• Daniel J. Müller and
• Jonne Helenius

Beilstein J. Nanotechnol. 2015, 6, 157–166, doi:10.3762/bjnano.6.15

• matrix proteins, fibronectin, collagen I and laminin 332, was examined. The adhesion of each cell line to different matrix proteins was found to be distinct; no two cell lines adhered equally to each of the proteins. The PDMS masks improved the throughput limitation of single-cell force spectroscopy and

• allowed for experiments that previously were not feasible. Since the masks are economical and versatile, they can aid in the improvement of various assays. Keywords: atomic force microscopy; cell adhesion; collagen I; fibroblasts; fibronectin; HeLa; laminin; MDCK; PC3; single cell assay; single cell

• CAM has been studied by SCFS. It was shown by SCFS that collagen I binding integrins down-regulate the avidity of fibronectin binding integrins by an increased endocytosis in HeLa cells [30]. The classical SCFS setup, where the adhesion of a cantilever-bound cell to a substrate is probed, has a

In vitro and in vivo interactions of selected nanoparticles with rodent serum proteins and their consequences in biokinetics

• Wolfgang G. Kreyling,
• Stefanie Fertsch-Gapp,
• Martin Schäffler,
• Blair D. Johnston,
• Nadine Haberl,
• Christian Pfeiffer,
• Jörg Diendorf,
• Carsten Schleh,
• Stephanie Hirn,
• Manuela Semmler-Behnke,
• Matthias Epple and
• Wolfgang J. Parak

Beilstein J. Nanotechnol. 2014, 5, 1699–1711, doi:10.3762/bjnano.5.180

• ; Cfh: complement component factor h; Mug1: murinoglobulin 1; Pzp: pregnancy zone protein; Itih4: inter alpha-trypsin inhibitor, heavy chain 4; Gsn: gelsolin; Ahsg: alpha-2-HS-glycoprotein; Fn1: fibronectin 1; Alb: albumin; C3: complement component 3. Schematics of the analysis of quantitative NP

Hydrophobic interaction governs unspecific adhesion of staphylococci: a single cell force spectroscopy study

• Nicolas Thewes,
• Peter Loskill,
• Philipp Jung,
• Henrik Peisker,
• Markus Bischoff,
• Mathias Herrmann and
• Karin Jacobs

Beilstein J. Nanotechnol. 2014, 5, 1501–1512, doi:10.3762/bjnano.5.163

• genome sequence of S. carnosus strain TM300 (deposited in the EMBL nucleotide database under accession number AM295250), 19 putative cell-wall anchored proteins harboring LPXTG motifs are predicted, including homologues of well-studied S. aureus adhesins such as clumping factor A and B, fibronectin

Model systems for studying cell adhesion and biomimetic actin networks

• Dorothea Brüggemann,
• Johannes P. Frohnmayer and
• Joachim P. Spatz

Beilstein J. Nanotechnol. 2014, 5, 1193–1202, doi:10.3762/bjnano.5.131

• , for instance fibronectin, vitronectin, fibrinogen or laminin, contain the tripeptide sequence arginine-glycine-aspartic acid (RGD), which is specifically recognised by most integrins [3][7][8]. The affinity as well as the specificity of integrins to bind to their ligands in the ECM can also be