PVP-coated, negatively charged silver nanoparticles: A multi-center study of their physicochemical characteristics, cell culture and in vivo experiments

• Sebastian Ahlberg,
• Alexandra Antonopulos,
• Jörg Diendorf,
• Ralf Dringen,
• Matthias Epple,
• Rebekka Flöck,
• Wolfgang Goedecke,
• Christina Graf,
• Nadine Haberl,
• Jens Helmlinger,
• Fabian Herzog,
• Frederike Heuer,
• Stephanie Hirn,
• Christian Johannes,
• Stefanie Kittler,
• Manfred Köller,
• Katrin Korn,
• Wolfgang G. Kreyling,
• Fritz Krombach,
• Jürgen Lademann,
• Kateryna Loza,
• Eva M. Luther,
• Marcelina Malissek,
• Martina C. Meinke,
• Daniel Nordmeyer,
• Anne Pailliart,
• Jörg Raabe,
• Fiorenza Rancan,
• Barbara Rothen-Rutishauser,
• Eckart Rühl,
• Carsten Schleh,
• Andreas Seibel,
• Christina Sengstock,
• Lennart Treuel,
• Annika Vogt,
• Katrin Weber and
• Reinhard Zellner

Beilstein J. Nanotechnol. 2014, 5, 1944–1965, doi:10.3762/bjnano.5.205

• , the dissolution rate is strongly increased. On the other hand, the dissolution is significantly slower in the presence of dissolved NaCl, a fact that may be due to the formation of insoluble silver chloride. An even stronger inhibiting effect is exerted by the sulfur-containing amino acid cysteine. We

• . As an early response to genomic DSB, a variant of histone H2A becomes phosphorylated at amino acid 139 by members of the PI3-kinase family in the direct vicinity of the break. The phosphorylated form of H2AX (γ-H2AX) is necessary to activate the DSB-repair machinery [117] and therefore, it can be

Protein-coated pH-responsive gold nanoparticles: Microwave-assisted synthesis and surface charge-dependent anticancer activity

• Dickson Joseph,
• Nisha Tyagi,
• Christian Geckeler and
• Kurt E.Geckeler

Beilstein J. Nanotechnol. 2014, 5, 1452–1462, doi:10.3762/bjnano.5.158

• and thereby deactivates some of the amino acid residues responsible for the reduction of the Au ions. Structural conformation The main objective of this work was the preparation of AuNPs by using proteins, not retaining the structural conformation of the proteins, because changes in the structural

• remaining proteins are expected to retain their amino acid sequence and not have extensive changes in their properties, such as their intrinsic pH and isoelectric points. Composition of amino acid residues Recent reports suggest that amino acid residues, such as aspartic acid, cysteine, glutamic acid

• , tyrosine and tryptophan, can reduce Au(III) and Ag(I) ions [12][18][38][41][42][43][44][45][46]. In this study, amino acid content of each protein is different due to differences in their molecular weights and amino acid sequences. Thus, predicting that a particular amino acid is responsible for the

Organic and inorganic–organic thin film structures by molecular layer deposition: A review

• Pia Sundberg and
• Maarit Karppinen

Beilstein J. Nanotechnol. 2014, 5, 1104–1136, doi:10.3762/bjnano.5.123

• and phenols” have also another functional group, such as 4-aminophenol with both –OH and –NH2 groups. (2S)-2-Aminopentanedioic acid, an amino acid with carboxylic acid functionality, is considered under “Acids”. “Other organic precursors” consist of all the organic precursors that do not fall clearly

• and FTIR experiments conducted for the crystallized films, the composition was close to that of MOF-5. Klepper et al. [112] used (2S)-2-aminopentanedioic acid, an amino acid with a carboxylic acid functional group, together with TMA. The films were grown in the temperature range of 200–350 °C. The GPC

Controlling mechanical properties of bio-inspired hydrogels by modulating nano-scale, inter-polymeric junctions

• Seonki Hong,
• Hyukjin Lee and
• Haeshin Lee

Beilstein J. Nanotechnol. 2014, 5, 887–894, doi:10.3762/bjnano.5.101

• quinones. For mussel adhesives, DOPAquinone is formed by oxidation of a catecholic amino acid, 3,4-dihydroxy-L-phenylalanine (DOPA). Subsequently, DOPAquinone rapidly reacts with basic amino acids, such as lysine and/or histidine, forming covalent adducts of DOPA-DOPA, lysyl-DOPA, and/or histeinyl-DOPA [7

Manipulation of isolated brain nerve terminals by an external magnetic field using D-mannose-coated γ-Fe₂O₃ nano-sized particles and assessment of their effects on glutamate transport

• Tatiana Borisova,
• Natalia Krisanova,
• Arsenii Borуsov,
• Roman Sivko,
• Ludmila Ostapchenko,
• Michal Babic and
• Daniel Horak

Beilstein J. Nanotechnol. 2014, 5, 778–788, doi:10.3762/bjnano.5.90

• that D-mannose-modified iron oxide nanoparticles could cross the cell membranes and be internalized by rat bone marrow stromal cells [12]. In the mammalian central nervous system, amino acid glutamate plays a primary role as a key excitatory neurotransmitter. Glutamate participates in many aspects of

Extracellular biosynthesis of gadolinium oxide (Gd₂O₃) nanoparticles, their biodistribution and bioconjugation with the chemically modified anticancer drug taxol

• Shadab Ali Khan,
• Sanjay Gambhir and
• Absar Ahmad

Beilstein J. Nanotechnol. 2014, 5, 249–257, doi:10.3762/bjnano.5.27

• secreted in the solution by the fungus Humicola sp. in response to the stress conditions encountered by the fungus in the presence of GdCl3. Some of these amino acid residues constitute the protein layer, which can cap the nanoparticles. As soon as GdCl3 gets dissolved in water along with fungal biomass

Nanoscopic surfactant behavior of the porin MspA in aqueous media

• Ayomi S. Perera,
• Hongwang Wang,
• Tej B. Shrestha,
• Deryl L. Troyer and
• Stefan H. Bossmann

Beilstein J. Nanotechnol. 2013, 4, 278–284, doi:10.3762/bjnano.4.30

• describes the energetic contribution arising from the interactions of the vestibules of MspA in the bilayer. Due to the presence of polar amino-acid side-chains at the exterior of the MspA’s “head”, hydrogen bonding [29] is most likely responsible for the discrepancy of the calculated packing parameter P

Detection of interaction between biomineralising proteins and calcium carbonate microcrystals

• Hanna Rademaker and
• Malte Launspach

Beilstein J. Nanotechnol. 2011, 2, 222–227, doi:10.3762/bjnano.2.26

• . These two protein bands (one at approx. 19 kDa and the other at about 25 kDa) belong to the protein perlucin [10]. The corresponding fractions of purified protein showing these two bands on SDS-PAGEs had been subjected to N-terminal amino acid sequence analysis [11] in several different experiments

• of perlucin has saccharide oligomers bound to these sites. In MALDI-MS (matrix-assisted laser desorption/ionization mass spectroscopy) of perlucin [10] variable molecular weights of perlucin are detectable, which can be related to a 10 amino acid repeat at the C-terminus being present in various

Electrochemical behavior of dye-linked L-proline dehydrogenase on glassy carbon electrodes modified by multi-walled carbon nanotubes

• Haitao Zheng,
• Leyi Lin,
• Yosuke Okezaki,
• Ryushi Kawakami,
• Haruhiko Sakuraba,
• Toshihisa Ohshima,
• Keiichi Takagi and
• Shin-ichiro Suye

Beilstein J. Nanotechnol. 2010, 1, 135–141, doi:10.3762/bjnano.1.16

• typical Michaelis–Menten catalytic response with lower apparent constant. Keywords: dye-linked L-proline dehydrogenase; electrocatalysis; electron transfer; multi-walled carbon nanotube; Introduction As an essential amino acid for the proper functioning of tendons and joints in the human body, the quick

• for the detection of various types of chemical or biochemical substances [18][19][20][21][22][23]. Some amino acid biosensors have already been reported based on CNTs-modified electrodes [24][25][26][27]. In our previous work, the recombinant thermostable dye-linked L-proline dehydrogenase (L-proDH