Toward an Optimal Joint Recognition of the S1‘ Subsites of Endothelin Converting Enzyme-1 (ECE-1), Angiotensin Converting Enzyme (ACE), and Neutral Endopeptidase (NEP)
摘要:
The formation of vasoconstrictors (e.g., angiotensin II and endothelin) and the inactivation of vasodilators (e.g., bradykinin and atrial natriuretic) by membrane-bound zinc metallopeptidases are key mechanisms in the control of blood pressure and fluid homeostasis. The way in which these peptides modulate physiological functions has been intensively studied. With the aim to develop compounds that can jointly block the three metallopeptidases-neutral endopeptidase (NEP, neprilysin), angiotensin-converting enzyme (ACE), and endothelin-converting enzyme (ECE-1)-we studied the common structural specificity of the S-1' subsites of these peptidases. Various mercaptoacyl amino acids of the general formula HS-CH2-CH(R-1')CO-Trp-OH, possessing more or less constrained R-1' side chains, were designed. The mercapto-acyl synthons contain one or two asymmetrical centers. The K-i values of the separated stereoisomers of the most efficient inhibitors were used to determine the stereochemical preference of each enzyme. A guideline for the joint inhibition of the three peptidases was obtained with the (2R,3R) isomer of compound 13b. Its K-i values on NEP, ACE, and ECE were 0.7, 43, and 26 nM, respectively.
Toward an Optimal Joint Recognition of the S1‘ Subsites of Endothelin Converting Enzyme-1 (ECE-1), Angiotensin Converting Enzyme (ACE), and Neutral Endopeptidase (NEP)
摘要:
The formation of vasoconstrictors (e.g., angiotensin II and endothelin) and the inactivation of vasodilators (e.g., bradykinin and atrial natriuretic) by membrane-bound zinc metallopeptidases are key mechanisms in the control of blood pressure and fluid homeostasis. The way in which these peptides modulate physiological functions has been intensively studied. With the aim to develop compounds that can jointly block the three metallopeptidases-neutral endopeptidase (NEP, neprilysin), angiotensin-converting enzyme (ACE), and endothelin-converting enzyme (ECE-1)-we studied the common structural specificity of the S-1' subsites of these peptidases. Various mercaptoacyl amino acids of the general formula HS-CH2-CH(R-1')CO-Trp-OH, possessing more or less constrained R-1' side chains, were designed. The mercapto-acyl synthons contain one or two asymmetrical centers. The K-i values of the separated stereoisomers of the most efficient inhibitors were used to determine the stereochemical preference of each enzyme. A guideline for the joint inhibition of the three peptidases was obtained with the (2R,3R) isomer of compound 13b. Its K-i values on NEP, ACE, and ECE were 0.7, 43, and 26 nM, respectively.
CONDUCTIVE PASTE AND MIXTURE PASTE FOR LITHIUM ION BATTERY POSITIVE ELECTRODE
申请人:KANSAI PAINT CO., LTD.
公开号:EP3168904A1
公开(公告)日:2017-05-17
The present invention provides a conductive paste for positive electrodes of lithium-ion batteries and mixture paste for positive electrodes of lithium-ion batteries that have an easy-to-apply viscosity, even when a relatively small amount of a dispersant is incorporated. More specifically, the present invention provides a conductive paste for positive electrodes of lithium-ion batteries containing a dispersion resin (A), conductive carbon (B), and a solvent (C), the dispersion resin (A) being a copolymer of a monomer mixture comprising a polycyclic aromatic hydrocarbon-containing monomer (A-1) in an amount of 1 to 70 mass%, based on the total solids content.
CONDUCTIVE PASTE FOR LITHIUM-ION BATTERY POSITIVE ELECTRODES AND MIXTURE PASTE FOR LITHIUM-ION BATTERY POSITIVE ELECTRODES
申请人:KANSAI PAINT CO., LTD.
公开号:EP3193398A1
公开(公告)日:2017-07-19
This invention relates to a conductive paste for lithium-ion battery positive electrodes and a mixture paste for a lithium ion battery positive electrode that have an easy-to-apply viscosity, even when a relatively small amount of a dispersion resin is incorporated. More specifically, the invention provides a conductive paste for lithium-ion battery positive electrodes, the conductive paste comprising a dispersion resin (A), conductive carbon (B), and a solvent (C), the dispersion resin (A) containing a resin (A1), the resin (A1) containing, as one constituent component, a polymerizable unsaturated group-containing monomer (A1-1) represented by a specific formula.
Conductive paste and mixture paste for lithium ion battery positive electrode
申请人:KANSAI PAINT CO., LTD.
公开号:US10256472B2
公开(公告)日:2019-04-09
The present invention provides a conductive paste for positive electrodes of lithium-ion batteries and mixture paste for positive electrodes of lithium-ion batteries that have an easy-to-apply viscosity, even when a relatively small amount of a dispersant is incorporated. More specifically, the present invention provides a conductive paste for positive electrodes of lithium-ion batteries containing a dispersion resin (A), conductive carbon (B), and a solvent (C), the dispersion resin (A) being a copolymer of a monomer mixture comprising a polycyclic aromatic hydrocarbon-containing monomer (A-1) in an amount of 1 to 70 mass %, based on the total solids content.
Conductive paste for lithium-ion battery positive electrodes and mixture paste for lithium-ion battery positive electrodes
申请人:KANSAI PAINT CO., LTD.
公开号:US10355281B2
公开(公告)日:2019-07-16
This invention relates to a conductive paste for lithium-ion battery positive electrodes and a mixture paste for a lithium ion battery positive electrode that have an easy-to-apply viscosity, even when a relatively small amount of a dispersion resin is incorporated. More specifically, the invention provides a conductive paste for lithium-ion battery positive electrodes, the conductive paste comprising a dispersion resin (A), conductive carbon (B), and a solvent (C), the dispersion resin (A) containing a resin (A1), the resin (A1) containing, as one constituent component, a polymerizable unsaturated group-containing monomer (A1-1) represented by a specific formula.
Toward an Optimal Joint Recognition of the S<sub>1</sub>‘ Subsites of Endothelin Converting Enzyme-1 (ECE-1), Angiotensin Converting Enzyme (ACE), and Neutral Endopeptidase (NEP)
作者:Nicolas Inguimbert、Pascale Coric、Hervé Poras、Hervé Meudal、Franck Teffot、Marie-Claude Fournié-Zaluski、Bernard P. Roques
DOI:10.1021/jm0005454
日期:2002.3.1
The formation of vasoconstrictors (e.g., angiotensin II and endothelin) and the inactivation of vasodilators (e.g., bradykinin and atrial natriuretic) by membrane-bound zinc metallopeptidases are key mechanisms in the control of blood pressure and fluid homeostasis. The way in which these peptides modulate physiological functions has been intensively studied. With the aim to develop compounds that can jointly block the three metallopeptidases-neutral endopeptidase (NEP, neprilysin), angiotensin-converting enzyme (ACE), and endothelin-converting enzyme (ECE-1)-we studied the common structural specificity of the S-1' subsites of these peptidases. Various mercaptoacyl amino acids of the general formula HS-CH2-CH(R-1')CO-Trp-OH, possessing more or less constrained R-1' side chains, were designed. The mercapto-acyl synthons contain one or two asymmetrical centers. The K-i values of the separated stereoisomers of the most efficient inhibitors were used to determine the stereochemical preference of each enzyme. A guideline for the joint inhibition of the three peptidases was obtained with the (2R,3R) isomer of compound 13b. Its K-i values on NEP, ACE, and ECE were 0.7, 43, and 26 nM, respectively.