Controlled Interfacial Permeation, Nanostructure Formation, Catalytic Efficiency, Signal Enhancement Capability, and Cell Spreading by Adjusting Photochemical Cross-Linking Degrees of Layer-by-Layer Films

2016 ◽  
Vol 8 (49) ◽  
pp. 34080-34088 ◽  
Author(s):  
Xinglong Luan ◽  
Tao Huang ◽  
Yan Zhou ◽  
Qi An ◽  
Yue Wang ◽  
...  
Keyword(s):  
Catalytic Efficiency ◽  
Cell Spreading ◽  
Signal Enhancement ◽  
Cross Linking ◽  
Layer By Layer ◽  
Nanostructure Formation

Radical-triggered cross-linking for molecular layer deposition of SiAlCOH hybrid thin films

2021 ◽  
Author(s):  
Kristina Ashurbekova ◽  
Karina Ashurbekova ◽  
Iva Saric ◽  
Evgeny Modin ◽  
Mladen Petravic ◽  
...  
Keyword(s):  
Thin Film ◽  
Film Growth ◽  
Molecular Layer ◽  
Thin Film Growth ◽  
Cross Linking ◽  
Layer By Layer ◽  
Molecular Layer Deposition ◽  
Layer Deposition ◽  
Hybrid Thin Films ◽  
Enhanced Stability

We developed a thin film growth with a radical-initiated cross-linking of vinyl groups in a layer-by-layer manner via molecular layer deposition (MLD). The cross-linked film exhibited improved properties like 12% higher density and enhanced stability compared to the non-cross-linked film.

Multilayer composite beads constructed via layer-by-layer self-assembly for lysozyme controlled release

RSC Advances ◽  
2014 ◽  
Vol 4 (46) ◽  
pp. 24369-24376 ◽  
Author(s):  
Jiemin Zhao ◽  
Xiaoping Wang ◽  
Yanshen Kuang ◽  
Yufeng Zhang ◽  
Xiaowen Shi ◽  
...  
Keyword(s):  
Controlled Release ◽  
Self Assembly ◽  
Cross Linking ◽  
Layer By Layer ◽  
Multilayer Composite ◽  
Composite Beads ◽  
Assembly Technique ◽  
Positively Charged

Alginate (ALG)–lysozyme (LZ) beads were fabricated by a cross-linking process. Negatively charged ALG and positively charged LZ were alternately deposited on the positively charged ALG–LZ beads via a layer-by-layer (LBL) self-assembly technique.

Cross-Linking Bi2S3Ultrathin Nanowires: A Platform for Nanostructure Formation and Biomolecule Detection

Nano Letters ◽  
2009 ◽  
Vol 9 (4) ◽  
pp. 1482-1486 ◽  
Author(s):  
Ludovico Cademartiri ◽  
Francesco Scotognella ◽  
Paul G. O’Brien ◽  
Bettina V. Lotsch ◽  
Jordan Thomson ◽  
...  
Keyword(s):  
Cross Linking ◽  
Biomolecule Detection ◽  
Nanostructure Formation

scholarly journals Studies on cell adhesion and recognition. II. The kinetics of cell adhesion and cell spreading on surfaces coated with carbohydrate-reactive proteins (glycosidases and lectins) and fibronectin.

1981 ◽  
Vol 88 (1) ◽  
pp. 138-148 ◽  
Author(s):  
W G Carter ◽  
H Rauvala ◽  
S I Hakomori
Keyword(s):  
Cell Adhesion ◽  
Cell Surface ◽  
Cell Attachment ◽  
Cell Spreading ◽  
Galactose Oxidase ◽  
Cross Linking ◽  
Con A ◽  
Coated Surfaces ◽  
Plastic Surfaces ◽  
Kinetics Of

The kinetics of cell attachment and cell spreading on the coated surfaces of two classes of carbohydrate-reactive proteins, enzymes and lectins, have been compared with those on fibronectin-coated surfaces with the following results: (a) A remarkable similarity between the kinetics of cell attachment to fibronectin-coated and glycosidase-coated surfaces was found. In contrast, cell attachment kinetics induced by lectin- and galactose oxidase-coated surfaces, in general, were strikingly different from those on fibronectin and glycosidase surfaces. The distinction between fibronectin- or glycosidase- and lectin- or galactose oxidase (an enzyme with lectin-type characteristics)-coated surfaces was further supported by the finding that cytochalasin B and EDTA inhibited cell attachment to fibronectin- and glycosidase-coated surfaces but not lectin-coated surfaces. (b) Fibronectin, if labeled and added to a cell suspension, showed only low or negligible interaction with the cell surface. However, fibronectin absorbed on plastic surfaces showed a high cell-attaching activity. It is assumed that fibronectin coated on plastic surfaces may form polyvalent attachment sites in contrast to its lower valency in aqueous solution. (c) Various inhibitors of cell attachment to both fibronectin-, galactose oxidase-, and lectin-coated surfaces were effective only during the first few minutes of the adhesion assay, after which time the attached cells became insensitive to the inhibitors. It is suggested that the initial specific recognition on either lectin-type or fibronectin-type surfaces is followed by an active cell-dependent attachment process. The primary role of the adhesion surface is to stimulate the cell-dependent attachment response. (d) Cells attached on tetravalent concanavalin A (Con A) spread very rapidly and quantitatively, whereas divalent succinyl Con A and monovalent Con A were effective stimulators of cell attachment but not cell spreading. Cross-linking of succinyl Con A restored the cell spreading activity. Tetravalent Con A surfaces specifically bind soluble glycoproteins, whereas succinyl Con A has a greatly reduced ability to bind the same glycoproteins. These results suggest that cross-linking of cell surface glycoproteins by the multivalent adhesive surface may trigger the cellular reaction leading to cell spreading.

scholarly journals Structure–function analyses of the G729R 2-oxoadipate dehydrogenase genetic variant associated with a disorder of l-lysine metabolism

2020 ◽  
Vol 295 (23) ◽  
pp. 8078-8095 ◽  
Author(s):  
Xu Zhang ◽  
Natalia S. Nemeria ◽  
João Leandro ◽  
Sander Houten ◽  
Michael Lazarus ◽  
...  
Keyword(s):  
Structure Function ◽  
Catalytic Efficiency ◽  
Reaction Rates ◽  
Cross Linking ◽  
Side Reactions ◽  
Systematic Analysis ◽  
Severe Intellectual Disability ◽  
Tryptophan Catabolism ◽  
Reduced Rate

2-Oxoadipate dehydrogenase (E1a, also known as DHTKD1, dehydrogenase E1, and transketolase domain-containing protein 1) is a thiamin diphosphate-dependent enzyme and part of the 2-oxoadipate dehydrogenase complex (OADHc) in l-lysine catabolism. Genetic findings have linked mutations in the DHTKD1 gene to several metabolic disorders. These include α-aminoadipic and α-ketoadipic aciduria (AMOXAD), a rare disorder of l-lysine, l-hydroxylysine, and l-tryptophan catabolism, associated with clinical presentations such as developmental delay, mild-to-severe intellectual disability, ataxia, epilepsy, and behavioral disorders that cannot currently be managed by available treatments. A heterozygous missense mutation, c.2185G→A (p.G729R), in DHTKD1 has been identified in most AMOXAD cases. Here, we report that the G729R E1a variant when assembled into OADHc in vitro displays a 50-fold decrease in catalytic efficiency for NADH production and a significantly reduced rate of glutaryl-CoA production by dihydrolipoamide succinyl-transferase (E2o). However, the G729R E1a substitution did not affect any of the three side-reactions associated solely with G729R E1a, prompting us to determine the structure–function effects of this mutation. A multipronged systematic analysis of the reaction rates in the OADHc pathway, supplemented with results from chemical cross-linking and hydrogen–deuterium exchange MS, revealed that the c.2185G→A DHTKD1 mutation affects E1a–E2o assembly, leading to impaired channeling of OADHc intermediates. Cross-linking between the C-terminal region of both E1a and G729R E1a with the E2o lipoyl and core domains suggested that correct positioning of the C-terminal E1a region is essential for the intermediate channeling. These findings may inform the development of interventions to counter the effects of pathogenic DHTKD1 mutations.

γ-Irradiation Induced Synthesis of Titanium Dioxide/Poly(acrylic acid) (TiO2/PAA) Nanocomposites and Layer-by-Layer Assembly on Glass Substrate

2015 ◽  
Vol 1098 ◽  
pp. 25-30 ◽  
Author(s):  
Lawrence John Paulo L. Trinidad ◽  
Ken Aldren S. Usman ◽  
Leon M. Payawan
Keyword(s):  
Acrylic Acid ◽  
Layer Thickness ◽  
Titania Nanoparticles ◽  
Cross Linking ◽  
Layer By Layer ◽  
Γ Irradiation ◽  
Sem Images ◽  
Nucleation Sites ◽  
Anatase Titania ◽  
Poly Acrylic Acid

Adsorption and encapsulation of the nanoparticles in polyelectrolytes impart stability to the nanometal by preventing aggregation through electrostatic and steric effects. Poly (acrylic acid) (PAA) was employed as a polymer cap to anatase titania nanoparticles. Cross-linking of the polymer was done via free-radical cross-linking using gamma-irradiation. The size of the nanocomposite produced ranged from 40-120 nm. SEM images showed that excess TiO2 in solution becomes nucleation sites for aggregation. Film assembly of the synthesized nanocomposite were done by layer-by-layer deposition with PDDA. Films formed with increasing thickness (5, 10, and 15 layers) were analyzed under AFM and shown to have a thickness of 0.25 μm, 1.1μm and 3.0 μm respectively.The average film layer thickness obtained ranged from 50-200 nm per TiO2/PAA-PDDA layer where as the number of layers deposited increase, the layer thickness increase while the roughness decreases.

scholarly journals Enhanced Performance of Immobilized Xylanase/Filter Paper-ase on a Magnetic Chitosan Support

Catalysts ◽  
2019 ◽  
Vol 9 (11) ◽  
pp. 966
Author(s):  
Aldo Amaro-Reyes ◽  
Azariel Díaz-Hernández ◽  
Jorge Gracida ◽  
Blanca E. García-Almendárez ◽  
Monserrat Escamilla-García ◽  
...  
Keyword(s):  
Filter Paper ◽  
Catalytic Efficiency ◽  
Cost Effective ◽  
Immobilized Enzymes ◽  
Hydrolytic Activity ◽  
Industrial Applications ◽  
Biochemical Properties ◽  
Free Form ◽  
Cross Linking ◽  
Magnetic Chitosan

Enzyme immobilization on different supports has emerged as an efficient and cost-effective tool to improve their stability and reuse capacity. This work aimed to produce a stable immobilized multienzymatic system of xylanase and filter paper-ase (FPase) onto magnetic chitosan using genipin as a cross-linking agent and to evaluate its biochemical properties and reuse capacity. A mixture of chitosan magnetic nanoparticles, xylanase, and FPase was covalently bonded using genipin. Immobilization yield and efficiency were quantified. The activity of free and immobilized enzymes was quantified at different values of pH, temperature, substrate concentration (Km and Vmax), and reuse cycles. The immobilization yield, immobilization efficiency, and activity recovery were 145.3% ± 3.06%, 14.8% ± 0.81%, and 21.5% ± 0.72%, respectively, measured as the total hydrolytic activity. Immobilization confers resistance to acidic/basic conditions and thermal stability compared to the free form. Immobilization improved 3.5-fold and 78-fold the catalytic efficiency (Kcat/Km) of the xylanase and filter paper-ase activities, while immobilized xylanase and FPase could be reused for 34 min and 43 min, respectively. Cross-linking significantly improved the biochemical properties of immobilized enzymes, combined with their simplicity of reuse due to the paramagnetic property of the support. Multienzyme immobilization technology is an important issue for industrial applications.

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