Nanoheterogeneous catalysis in electrochemically induced olefin perfluoroalkylation

2015 ◽  
Vol 44 (19) ◽  
pp. 8833-8838 ◽  
Author(s):  
Yulia B. Dudkina ◽  
Tatyana V. Gryaznova ◽  
Yuri N. Osin ◽  
Vadim V. Salnikov ◽  
Nikolay A. Davydov ◽  
...  
Keyword(s):  
Silica Nanoparticles ◽  
Amino Groups ◽  
Nanoheterogeneous Catalysis ◽  
P Immobilization

Immobilization of a (bpy)NiBr2complex on silica nanoparticles decorated with anchoring amino-groups was used to perform Ni-catalyzed electroreductive olefin perfluoroalkylation.

scholarly journals Immobilization of an artificial imine reductase within silica nanoparticles improves its performance

2016 ◽  
Vol 52 (60) ◽  
pp. 9462-9465 ◽  
Author(s):  
Martina Hestericová ◽  
M. Rita Correro ◽  
Markus Lenz ◽  
Philippe F.-X. Corvini ◽  
Patrick Shahgaldian ◽  
...  
Keyword(s):  
Silica Nanoparticles ◽  
P Immobilization

Immobilization and protection of artificial imine reductase in silica nanoparticles increases its activity and protects from various denaturing stresses.

scholarly journals Mesoporous Silica Nanoparticles Functionalized with Amino Groups for Biomedical Applications

ChemistryOpen ◽  
2021 ◽  
Vol 10 (12) ◽  
pp. 1251-1259
Author(s):  
Bianca Martins Estevão ◽  
Ivana Miletto ◽  
Noboru Hioka ◽  
Leonardo Marchese ◽  
Enrica Gianotti
Keyword(s):  
Mesoporous Silica ◽  
Silica Nanoparticles ◽  
Biomedical Applications ◽  
Mesoporous Silica Nanoparticles ◽  
Amino Groups

scholarly journals Effect of amino groups of mesoporous silica nanoparticles on CpG oligodexynucleotide delivery

2015 ◽  
Vol 16 (4) ◽  
pp. 045006 ◽  
Author(s):  
Yi Xu ◽  
Peter Claiden ◽  
Yufang Zhu ◽  
Hiromi Morita ◽  
Nobutaka Hanagata
Keyword(s):  
Mesoporous Silica ◽  
Silica Nanoparticles ◽  
Mesoporous Silica Nanoparticles ◽  
Amino Groups

scholarly journals Quantitative Analysis and Efficient Surface Modification of Silica Nanoparticles

2012 ◽  
Vol 2012 ◽  
pp. 1-8 ◽  
Author(s):  
Hak-Sung Jung ◽  
Doo-Sik Moon ◽  
Jin-Kyu Lee
Keyword(s):  
Surface Modification ◽  
Silica Nanoparticles ◽  
Functional Groups ◽  
Amino Groups ◽  
Modified Silica ◽  
Back Titration ◽  
Modified Silica Nanoparticles ◽  
Surface Modified ◽  
Rhodamine B Isothiocyanate ◽  
Absorption Measurements

Aminofunctional trialkoxysilanes such as aminopropyltrimethoxysilane (APTMS) and (3-trimethoxysilylpropyl)diethylenetriamine (DETAS) were employed as a surface modification molecule for generating monolayer modification on the surface of silica (SiO2) nanoparticles. We were able to quantitatively analyze the number of amine functional groups on the modified SiO2nanoparticles by acid-base back titration method and determine the effective number of amine functional groups for the successive chemical reaction by absorption measurements after treating with fluorescent rhodamine B isothiocyanate (RITC) molecules. The numbers of amine sites measured by back titration were 2.7 and 7.7 ea/nm2for SiO2-APTMS and SiO2-DETAS, respectively, while the numbers of effective amine sites measured by absorption calibration were about one fifth of the total amine sites, namely, 0.44 and 1.3 ea/nm2for SiO2-APTMS(RITC) and SiO2-DETAS(RITC), respectively. Furthermore, it was confirmed that the reactivity of amino groups on the surface-modified silica nanoparticles could be maintained in ethanol for more than 1.5 months without showing any significant differences in the reactivity.

Hyaluronic Acid Functionalized Porous Silica Nanoparticles for Drug Delivery and Release

2014 ◽  
Vol 936 ◽  
pp. 322-326
Author(s):  
Ling Yuan Cui ◽  
Yan Hui Li ◽  
Wei Zhang ◽  
Jing Peng Zhang ◽  
Qian Duan
Keyword(s):  
Hyaluronic Acid ◽  
Silica Nanoparticles ◽  
Drug Carrier ◽  
Porous Silica ◽  
Cancer Targeting ◽  
Nano Silica ◽  
Amino Groups ◽  
Model Drug ◽  
Site Selective ◽  
New Generation

In this paper, we reported a facile strategy to synthesize hyaluronic acid (HA) conjugated porous silica nanoparticles (pSiO2) as drug carrier. The pSiO2 were prepared by solid nano-silica nanoparticles with “surface-protected etching”. Morphologies of solid and porous silica nanoparticles were characterized by SEM and TEM. Amino groups were introduced on pSiO2 to graft HA as cancer targeting ligand. Then rifampicin used as model drug was loaded in pSiO2-HA. The results indicate that pSiO2 can perform a certain degree of slow release. Overall, the system might open the door to a new generation of carrier system for site-selective, controlled-release delivery of anticancer drugs.

Aldehyde gold clusters for molecular labeling

1995 ◽  
Vol 53 ◽  
pp. 858-859
Author(s):  
James F. Hainfeld ◽  
Frederic R. Furuya
Keyword(s):  
Covalent Bond ◽  
Aldehyde Group ◽  
Gold Clusters ◽  
Side Reactions ◽  
Amino Groups ◽  
Sodium Cyanoborohydride ◽  
Schiff’S Base ◽  
Protein Molecules ◽  
Hydroxysuccinimide Esters ◽  
Primary Amino

Glutaraldehyde is a useful tissue and molecular fixing reagents. The aldehyde moiety reacts mainly with primary amino groups to form a Schiff's base, which is reversible but reasonably stable at pH 7; a stable covalent bond may be formed by reduction with, e.g., sodium cyanoborohydride (Fig. 1). The bifunctional glutaraldehyde, (CHO-(CH2)3-CHO), successfully stabilizes protein molecules due to generally plentiful amines on their surface; bovine serum albumin has 60; 59 lysines + 1 α-amino. With some enzymes, catalytic activity after fixing is preserved; with respect to antigens, glutaraldehyde treatment can compromise their recognition by antibodies in some cases. Complicating the chemistry somewhat are the reported side reactions, where glutaraldehyde reacts with other amino acid side chains, cysteine, histidine, and tyrosine. It has also been reported that glutaraldehyde can polymerize in aqueous solution. Newer crosslinkers have been found that are more specific for the amino group, such as the N-hydroxysuccinimide esters, and are commonly preferred for forming conjugates. However, most of these linkers hydrolyze in solution, so that the activity is lost over several hours, whereas the aldehyde group is stable in solution, and may have an advantage of overall efficiency.

Microscopy study on the interaction of silica nanoparticles with lung epithelial cells

Pneumologie ◽  
2013 ◽  
Vol 67 (12) ◽  
Author(s):  
H Peuschel ◽  
T Ruckelshausen ◽  
C Cavelius ◽  
A Kraegeloh
Keyword(s):  
Epithelial Cells ◽  
Silica Nanoparticles ◽  
Microscopy Study ◽  
Lung Epithelial Cells ◽  
Lung Epithelial

The Action of Thrombin on Modified Fibrinogen

1983 ◽  
Vol 49 (03) ◽  
pp. 208-213
Author(s):  
A J Osbahr
Keyword(s):  
Physical Properties ◽  
Negative Charge ◽  
Lysine Residue ◽  
Fibrinopeptide A ◽  
Amino Groups ◽  
Lysine Residues ◽  
Citraconic Anhydride

SummaryThe modification of canine fibrinogen with citraconic anhydride modified the ε-amino groups of the fibrinogen and at the same time generated additional negative charges into the protein. The addition of thrombin to the modified fibrinogen did not induce polymerization; however, the fibrinopeptide was released at a faster rate than from the unmodified fibrinogen. The physical properties of the citraconylated fibrinogen were markedly altered by the modification of 50-60 lysine residues in one hour. A modified fibrinopeptide-A was released by thrombin from the modified fibrinogen and was electrophoretically more anionic than the unmodified fibrinopeptide-A. Edman analysis confirmed the modification of the lysine residue present in the peptide. The rate of removal of citraconylated fibrinopeptide-A from modified fibrinogen by thrombin was 30 to 40 percent greater than the cleavage of unmodified fibrinopeptide-A from unmodified fibrinogen. However, the modification of 60 or more lysine residues in the fibrinogen produced a decrease in the rate of cleavage of citraconylated fibrinopeptide-A. The results suggest that additional negative charge in the vicinity of the attachment of fibrinopeptide-A to canine fibrinogen aids in the removal of the peptide by thrombin.

COMPARATIVE STUDIES OF THE POTENTIATION OF CORTICOTROPHIN ACTIVITY BY SEVERAL INACTIVE DERIVATIVES

1963 ◽  
Vol 42 (2) ◽  
pp. 209-213 ◽  
Author(s):  
Arthur I. Cohen ◽  
Edward H. Frieden
Keyword(s):  
Biological Activity ◽  
Comparative Studies ◽  
Free Amino ◽  
Hormonal Activity ◽  
Amino Groups

ABSTRACT A number of corticotrophin analogues have been prepared, some of which potentiate the biological activity of the untreated hormone in vitro. The free amino groups of corticotrophin appear to be essential not only for hormonal activity, but also for the interaction of the analogues with the tissue corticotrophin inactivating system which is assumed to account for the potentiating effect.

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