scholarly journals Kinetic analysis of bioorthogonal reaction mechanisms using Raman microscopy

2019 ◽  
Vol 220 ◽  
pp. 71-85 ◽  
Author(s):  
William J. Tipping ◽  
Martin Lee ◽  
Valerie G. Brunton ◽  
Guy C. Lloyd-Jones ◽  
Alison N. Hulme
Keyword(s):  
Kinetic Analysis ◽  
Reaction Mechanisms ◽  
Raman Microscopy ◽  
Bioorthogonal Reaction ◽  
Bioorthogonal Reactions ◽  
Silent Region

Kinetic analysis of CuAAC and Glaser–Hay bioorthogonal reactions can be achieved with Raman microscopy using alkyne vibrations in the cell-silent region.

7 Tetrazine-Based Cycloadditions in Click Chemistry

2022 ◽  
Author(s):  
W. Kuba ◽  
M. Wilkovitsch ◽  
J. C. T. Carlson ◽  
H. Mikula
Keyword(s):  
Reaction Mechanisms ◽  
Chemical Biology ◽  
Bond Cleavage ◽  
Therapeutic Strategies ◽  
Complex Environments ◽  
Bioorthogonal Chemistry ◽  
Bioorthogonal Reaction ◽  
Low Concentrations ◽  
Time Critical

AbstractThe spontaneous cycloaddition of tetrazines with a number of different dienophiles has become a powerful tool in chemical biology, in particular for the biocompatible conjugation and modification of (bio)molecules. The exceptional reaction kinetics made these bioorthogonal ligations the methods of choice for time-critical processes at very low concentrations, facilitating controlled molecular transformations in complex environments and even in vivo. The emerging concept of bond-cleavage reactions triggered by tetrazine-based cycloadditions enabled the design of diagnostic and therapeutic strategies. The tetrazine-triggered activation of prodrugs represents the first bioorthogonal reaction performed in humans, marking the beginning of the era of clinical translation of bioorthogonal chemistry. This chapter provides an overview of the synthesis and reactivity of tetrazines, their cycloadditions with various dienophiles, and transformations triggered by these reactions, focusing on reaction mechanisms, kinetics and efficiency, and selected applications.

Études des réactions d'oxydation du n-heptane et de l'isooctane

1996 ◽  
Vol 74 (7) ◽  
pp. 1391-1402 ◽  
Author(s):  
Yves Simon ◽  
Gérard Scacchi ◽  
François Baronnet
Keyword(s):  
Experimental Study ◽  
Kinetic Analysis ◽  
Key Words ◽  
Reaction Mechanisms ◽  
Oxidation Reaction ◽  
Product Formation ◽  
Chemical Mechanism ◽  
Stirred Reactor ◽  
Oxidation Mechanisms

The oxidation mechanisms of two alkanes that have quite different octane numbers: n-heptane (0) and isooctane (100), were investigated to obtain a better understanding of the chemical mechanism of autoignition phenomena and to improve the compatibility of the available fuels with the engines. The experimental study was performed at 923 K in a setup equipped with a jet-stirred reactor. The oxidation mechanisms of n-heptane and isooctane were simplified first by a purely kinetic analysis based on the product formation and then by using a software of simulation of reaction mechanisms. The very different behaviour of these two hydrocarbons was explained by the presence, in the products of isooctane oxidation, of alkenes, which would have an antiknock effect due to the formation of resonance-stabilized radicals. Key words: oxidation reaction, n-heptane, isooctane, autoignition, modelling.

scholarly journals Multistage kinetic analysis of DMAA/MBAM polymer removal from gelcast ceramic parts using a multi-stage parallel reaction model and model-free method

RSC Advances ◽  
2019 ◽  
Vol 9 (47) ◽  
pp. 27305-27317 ◽  
Author(s):  
Jing Li ◽  
Jindi Huang ◽  
Ruiming Yin
Keyword(s):  
Kinetic Analysis ◽  
Reaction Mechanisms ◽  
Reaction Model ◽  
Parallel Reaction ◽  
Model Free ◽  
Multi Stage

This work aims to develop an effective method to investigate the multistage debinding kinetics and the reaction mechanisms of removing DMAA/MBAM polymer from gelcast ceramic parts.

Modeling of Enzyme Reaction Kinetics

1976 ◽  
Vol 98 (3) ◽  
pp. 266-269
Author(s):  
A. Cheruy
Keyword(s):  
Kinetic Analysis ◽  
Reaction Kinetics ◽  
Reaction Mechanisms ◽  
Enzyme Reaction ◽  
Enzymatic Reactions

It is shown in this paper how a kinetic analysis of enzymatic reactions with the goal of determining their reaction mechanisms corresponds to the modeling of a certain class of processes. Typical problems of these biosystems are discussed.

scholarly journals IEDDA: An Attractive Bioorthogonal Reaction for Biomedical Applications

Molecules ◽  
2021 ◽  
Vol 26 (15) ◽  
pp. 4640
Author(s):  
Maryana Handula ◽  
Kuo-Ting Chen ◽  
Yann Seimbille
Keyword(s):  
Biomedical Applications ◽  
Diels Alder ◽  
Staudinger Ligation ◽  
Bioorthogonal Reaction ◽  
Trans Conformation ◽  
Inverse Electron Demand ◽  
Bioorthogonal Reactions ◽  
Slow Kinetics ◽  
Direct Targeting ◽  
Electron Demand

The pretargeting strategy has recently emerged in order to overcome the limitations of direct targeting, mainly in the field of radioimmunotherapy (RIT). This strategy is directly dependent on chemical reactions, namely bioorthogonal reactions, which have been developed for their ability to occur under physiological conditions. The Staudinger ligation, the copper catalyzed azide-alkyne cycloaddition (CuAAC) and the strain-promoted [3 + 2] azide–alkyne cycloaddition (SPAAC) were the first bioorthogonal reactions introduced in the literature. However, due to their incomplete biocompatibility and slow kinetics, the inverse-electron demand Diels-Alder (IEDDA) reaction was advanced in 2008 by Blackman et al. as an optimal bioorthogonal reaction. The IEDDA is the fastest bioorthogonal reaction known so far. Its biocompatibility and ideal kinetics are very appealing for pretargeting applications. The use of a trans-cyclooctene (TCO) and a tetrazine (Tz) in the reaction encouraged researchers to study them deeply. It was found that both reagents are sensitive to acidic or basic conditions. Furthermore, TCO is photosensitive and can be isomerized to its cis-conformation via a radical catalyzed reaction. Unfortunately, the cis-conformer is significantly less reactive toward tetrazine than the trans-conformation. Therefore, extensive research has been carried out to optimize both click reagents and to employ the IEDDA bioorthogonal reaction in biomedical applications.

Analyzing reactions of single mechanoenzyme molecules by light microscopy

1992 ◽  
Vol 50 (1) ◽  
pp. 426-427
Author(s):  
Jeff Gelles
Keyword(s):  
Image Processing ◽  
Reaction Mechanisms ◽  
Transient State ◽  
Nanometer Scale ◽  
Reaction Intermediates ◽  
Enzyme Molecule ◽  
Directed Movement ◽  
Enzyme Molecules ◽  
Individual Enzyme ◽  
Single Reaction

Mechanoenzymes are enzymes which use a chemical reaction to power directed movement along biological polymer. Such enzymes include the cytoskeletal motors (e.g., myosins, dyneins, and kinesins) as well as nucleic acid polymerases and helicases. A single catalytic turnover of a mechanoenzyme moves the enzyme molecule along the polymer a distance on the order of 10−9 m We have developed light microscope and digital image processing methods to detect and measure nanometer-scale motions driven by single mechanoenzyme molecules. These techniques enable one to monitor the occurrence of single reaction steps and to measure the lifetimes of reaction intermediates in individual enzyme molecules. This information can be used to elucidate reaction mechanisms and determine microscopic rate constants. Such an approach circumvents difficulties encountered in the use of traditional transient-state kinetics techniques to examine mechanoenzyme reaction mechanisms.

X-Ray Microanalysis of Nickel and Cobalt Intensified Peroxidase- Antiperoxidase For Verification of Reaction Sites

1985 ◽  
Vol 43 ◽  
pp. 468-469
Author(s):  
A. Angel ◽  
K. Miller ◽  
V. Seybold ◽  
R. Kriebel
Keyword(s):  
Reaction Mechanisms ◽  
Visual Discrimination ◽  
Osmium Tetroxide ◽  
Ultrastructural Level ◽  
Microscopic Level ◽  
Electron Microscopic Level ◽  
Electron Microscopic ◽  
X Ray ◽  
Insoluble Polymer ◽  
Cytochemical Reaction

Localization of specific substances at the ultrastructural level is dependent on the introduction of chemicals which will complex and impart an electron density at specific reaction sites. Peroxidase-antiperoxidase(PAP) methods have been successfully applied at the electron microscopic level. The PAP complex is localized by addition of its substrate, hydrogen peroxide and an electron donor, usually diaminobenzidine(DAB). On oxidation, DAB forms an insoluble polymer which is able to chelate with osmium tetroxide becoming electron dense. Since verification of reactivity is visual, discrimination of reaction product from osmiophillic structures may be difficult. Recently, x-ray microanalysis has been applied to examine cytochemical reaction precipitates, their distribution in tissues, and to study cytochemical reaction mechanisms. For example, immunoreactive sites labelled with gold have been ascertained by means of x-ray microanalysis.

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