“Sticky invasion” – the physical properties of Plantago lanceolata L. seed mucilage

• Agnieszka Kreitschitz,
• Alexander Kovalev and
• Stanislav N. Gorb

Beilstein J. Nanotechnol. 2016, 7, 1918–1927, doi:10.3762/bjnano.7.183

• fibrils in the mucilage, which are responsible for a continuous and even distribution of the mucilaginous layer on the seed surface. The measured values of adhesive and frictional properties differed significantly in comparison to the previously studied pectic mucilage of Linum usitatissimum. Also, the

• water loss from the cellulose mucilage was more rapid. The obtained different values can result from the presence of cellulose fibrils and their interaction with pectins in the mucilage. Because of this feature the mucilage of P. lanceolata may represent a more regularly ordered and stabile system than

• wall that is rich in pectins form elastic, gel-like mucilage envelope after hydration [14][17]. Other components of the mucilage envelope such as cellulose fibrils also influence its properties and consequently its function. Seed mucilage possesses a clearly defined nanostructure. Cellulose is a linear

Functional diversity of resilin in Arthropoda

• Jan Michels,
• Esther Appel and
• Stanislav N. Gorb

Beilstein J. Nanotechnol. 2016, 7, 1241–1259, doi:10.3762/bjnano.7.115

• connected to the humeral angle of the anterior part of the wing base. The prealar arm consists of around 23% chitin and 77% resilin and is structured by alternating layers of resilin and chitin fibrils, with the fibrils continuing into the dark, sclerotised cuticle at its base [5] (Figure 1B). Due to the

• directional arrangement of chitin fibrils, the mechanical behaviour of the prealar arm is assumed to be dominated by the mechanical properties of the chitin fibrils during stretching and by the properties of resilin during bending and compression [5][11]. In contrast to the subalar muscle, which is involved

• organisation [23] (Figure 6A–D). Both pads possess a flexible resilin-containing exocuticle with fibrils that are fused into relatively large rods oriented in an angle to the surface. However, slight differences in the pad architecture exist. Adhesive pads of L. migratoria feature a clearly thicker superficial

Frog tongue surface microstructures: functional and evolutionary patterns

• Thomas Kleinteich and
• Stanislav N. Gorb

Beilstein J. Nanotechnol. 2016, 7, 893–903, doi:10.3762/bjnano.7.81

• adhesive mechanism of the tongue in the frog Ceratophrys ornata [13]. We suggested that the papillae increase the adaptability of the tongue to uneven surfaces and may help to form and anchor fibrils of mucus that emerge before a frog tongue is about to loose the contact with a target surface. While it has

Tattoo ink nanoparticles in skin tissue and fibroblasts

• Colin A. Grant,
• Peter C. Twigg,
• Richard Baker and
• Desmond J. Tobin

Beilstein J. Nanotechnol. 2015, 6, 1183–1191, doi:10.3762/bjnano.6.120

• . Not only can the AFM be used to visualise the surfaces of a wide range of materials (under various environmental conditions and over a large temperature range) the probe can also be used as a nano-indenter to ascertain mechanical properties [20] or even to carry out tensile testing of fibrils [21] or

• toxicological effects tattoo ink components may have on cells, collagen fibrils etc. because of their nanometre-scale size. A gram of 60.7 nm carbon spheres would have a surface area of about 40 m2; over 100000 times larger than the surface area of the equivalent bulk material. In addition, materials are known

• with a surface roughness Ra of 30 nm over the 10 μm scan region. The collagen fibrils here have a strong degree of parallel orientation, which would suggest that this region may well be scar tissue that was formed following the tattoo process. In a recent AFM study we compared scar tissue and healthy

Functionalization of α-synuclein fibrils

• Simona Povilonienė,
• Vida Časaitė,
• Virginijus Bukauskas,
• Arūnas Šetkus,
• Juozas Staniulis and
• Rolandas Meškys

Beilstein J. Nanotechnol. 2015, 6, 124–133, doi:10.3762/bjnano.6.12

• in the development of novel nanomaterials. Under certain conditions, amyloid protein α-synuclein forms well-ordered structures – fibrils, which have proven to be valuable building blocks for bionanotechnological approaches. Herein we demonstrate the functionalization of fibrils formed by a mutant α

• -synuclein that contains an additional cysteine residue. The fibrils have been biotinylated via thiol groups and subsequently joined with neutravidin-conjugated gold nanoparticles. Atomic force microscopy and transmission electron microscopy confirmed the expected structure – nanoladders. The ability of

• fibrils (and of the additional components) to assemble into such complex structures offers new opportunities for fabricating novel hybrid materials or devices. Keywords: α-synuclein; atomic force microscopy; gold nanoparticles; nanostructures; self-assembly; Introduction Due to their ability to form

Biocalcite, a multifunctional inorganic polymer: Building block for calcareous sponge spicules and bioseed for the synthesis of calcium phosphate-based bone

• Xiaohong Wang,
• Heinz C. Schröder and
• Werner E. G. Müller

Beilstein J. Nanotechnol. 2014, 5, 610–621, doi:10.3762/bjnano.5.72

• process between osteoblasts and fibrillar organic structures that starts from collagen fibrils around which poorly crystalline carbonated apatite aggregates are deposited [25][26]. Carbonated apatite are deposits in which carbonate ions (CO32−) reversibly substitute either phosphate (PO43−) or hydroxyl

Exploring the complex mechanical properties of xanthan scaffolds by AFM-based force spectroscopy

• Hao Liang,
• Guanghong Zeng,
• Yinli Li,
• Shuai Zhang,
• Huiling Zhao,
• Lijun Guo,
• Bo Liu and
• Mingdong Dong

Beilstein J. Nanotechnol. 2014, 5, 365–373, doi:10.3762/bjnano.5.42

• suggests complicated intermolecular interactions among xanthan fibrils. The results provide crucial information to understand the structures and mechanical properties of the xanthan scaffold. Keywords: atomic force microscopy (AFM); force spectroscopy (FS); mechanical properties; xanthan scaffold

• morphologies of xanthan-based materials, such as fibrils, networks [4] and ring-like structures [5], have been revealed by AFM imaging. Furthermore, AFM is a powerful tool for studying the mechanical properties on the nanoscale. AFM-based force spectroscopy (FS) has been applied to investigate the fingerprint

• identification of the rupture force and the characteristic separation distance in the proteins [30]. In addition, the investigation of the mechanical properties of denatured and native polysaccharides such as xanthan fibrils has been carried out carefully [31]. Force plateaus were observed during the stretching

Controlled synthesis and tunable properties of ultrathin silica nanotubes through spontaneous polycondensation on polyamine fibrils

• Jian-Jun Yuan,
• Pei-Xin Zhu,
• Daisuke Noda and
• Ren-Hua Jin

Beilstein J. Nanotechnol. 2013, 4, 793–804, doi:10.3762/bjnano.4.90

• crystalline fibrils that were conveniently produced from the neutralization of a solution of protonated linear polyethyleneimine (LPEI–H+) by alkali compounds. A simple mixing the fibrils with alkoxysilane in aqueous solution allowed for the rapid formation of silica to produce LPEI@silica hybrid nanotubes

• biosilicification [18][19]. Therefore, a number of strategies to design self-assembled organic aggregates has been developed in order to make these organic matrices work as templates/scaffolds/catalysts for a deposition of silica at ambient conditions [20]. Recently, self-assembled fibrils of polypeptides [21][22

• neutralization of LPEI–H+, which was absorbed at the substrate before [37]. That is, the substrate was dipped into an aqueous solution of LPEI–H+ to adsorb the polymers and then dipped into alkali solution for the neutralization. This self-assembly provided very thin films of LPEI fibrils that allowed for the

Molecular dynamics simulations of mechanical failure in polymorphic arrangements of amyloid fibrils containing structural defects

• Hlengisizwe Ndlovu,
• Alison E. Ashcroft,
• Sheena E. Radford and
• Sarah A. Harris

Beilstein J. Nanotechnol. 2013, 4, 429–440, doi:10.3762/bjnano.4.50

• , Leeds LS2 9JT, UK 10.3762/bjnano.4.50 Abstract We examine how the different steric packing arrangements found in amyloid fibril polymorphs can modulate their mechanical properties using steered molecular dynamics simulations. Our calculations demonstrate that for fibrils containing structural defects

• , their ability to resist force in a particular direction can be dominated by both the number and molecular details of the defects that are present. The simulations thereby suggest a hierarchy of factors that govern the mechanical resilience of fibrils, and illustrate the general principles that must be

• considered when quantifying the mechanical properties of amyloid fibres containing defects. Keywords: amyloid; fibril fragmentation; steered molecular dynamics (SMD); structural defects; Introduction Amyloid fibrils are biomaterials that are commonly associated with human disease [1]. Over recent years

Dimer/tetramer motifs determine amphiphilic hydrazine fibril structures on graphite

• Loji K. Thomas,
• Nadine Diek,
• Uwe Beginn and
• Michael Reichling

Beilstein J. Nanotechnol. 2012, 3, 658–666, doi:10.3762/bjnano.3.75

• –graphite interface by self-assembly of custom-designed symmetric and asymmetric amphiphilic benzamide derivatives bearing C10 aliphatic chains. Scanning tunnelling microscopy (STM) studies reveal geometry-dependent internal structures for the elementary fibrils of the two molecules that are distinctly

• different from known mesophase bulk structures. The structures are described by building-block models based on hydrogen-bonded dimer and tetramer precursors of hydrazines. The closure and growth in length of building units into fibrils takes place through van der Waals forces acting between the dangling

• alkyl chains. The nanoscale morphology is a consequence of the basic molecular geometry, where it follows that a closure to form a fibril is not always likely for the doubly substituted hydrazine. Therefore, we also observe crystallite formation. Keywords: fibrils; graphite; hydrazide; hydrazine

Nano-FTIR chemical mapping of minerals in biological materials

• Sergiu Amarie,
• Paul Zaslansky,
• Yusuke Kajihara,
• Erika Griesshaber,
• Wolfgang W. Schmahl and
• Fritz Keilmann

Beilstein J. Nanotechnol. 2012, 3, 312–323, doi:10.3762/bjnano.3.35

• 0.12 nm resolution (Figure 7c), the brightness provides a local measure of the electron density [48] and consequently of the mineral content [39]. While the white hypermineralized rim of the tubule exhibits an identical shape to that seen in the infrared (Figure 7b), the fine linear fibrils in the BEI

Self-organizing bioinspired oligothiophene–oligopeptide hybrids

• Alexey K. Shaytan,
• Eva-Kathrin Schillinger,
• Elena Mena-Osteritz,
• Sylvia Schmid,
• Pavel G. Khalatur,
• Peter Bäuerle and
• Alexei R. Khokhlov

Beilstein J. Nanotechnol. 2011, 2, 525–544, doi:10.3762/bjnano.2.57

• stable fibrils as visualized by AFM and TEM. While the experimental evidence alone is not sufficient to reveal the exact molecular organization of the fibrils, theoretical approaches based on quantum chemistry calculations and large-scale atomistic molecular dynamics simulations are attempted in an

• effort to reveal the structure of the fibrils at the nanoscale. Based on the combined theoretical and experimental analysis, the most likely models of fibril formation and aggregation are suggested. Keywords: amyloid-like fibrils; bioinspired conjugates; molecular dynamics simulations; oligopeptides

• applications as building blocks in nano- and biotechnology. Understanding the molecular details of peptide self-assembly into fibrillar aggregates has been a challenge owing to the large size, low solubility, and the noncrystalline and heterogeneous nature of the fibrils. During the last decade, considerable