Your browser doesn't support javascript.
loading
Mostrar: 20 | 50 | 100
Resultados 1 - 2 de 2
Filtrar
Mais filtros










Base de dados
Intervalo de ano de publicação
1.
ACS Omega ; 8(13): 11643-11664, 2023 Apr 04.
Artigo em Inglês | MEDLINE | ID: mdl-37033841

RESUMO

Technological and medical advances over the past few decades epitomize human capabilities. However, the increased life expectancies and concomitant land-use changes have significantly contributed to the release of ∼830 gigatons of CO2 into the atmosphere over the last three decades, an amount comparable to the prior two and a half centuries of CO2 emissions. The United Nations has adopted a pledge to achieve "net zero", i.e., yearly removing as much CO2 from the atmosphere as the amount emitted due to human activities, by the year 2050. Attaining this goal will require a concerted effort by scientists, policy makers, and industries all around the globe. The development of novel materials on industrial scales to selectively remove CO2 from mixtures of gases makes it possible to mitigate CO2 emissions using a multipronged approach. Broadly, the CO2 present in the atmosphere can be captured using materials and processes for biological, chemical, and geological technologies that can sequester CO2 while also reducing our dependence on fossil-fuel reserves. In this review, we used the curated literature available in the CAS Content Collection to present a systematic analysis of the various approaches taken by scientists and industrialists to restore carbon balance in the environment. Our analysis highlights the latest trends alongside the associated challenges.

2.
J Enzyme Inhib Med Chem ; 35(1): 1387-1402, 2020 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-32633155

RESUMO

Aza-peptide aldehydes and ketones are a new class of reversible protease inhibitors that are specific for the proteasome and clan CD cysteine proteases. We designed and synthesised aza-Leu derivatives that were specific for the chymotrypsin-like active site of the proteasome, aza-Asp derivatives that were effective inhibitors of caspases-3 and -6, and aza-Asn derivatives that inhibited S. mansoni and I. ricinus legumains. The crystal structure of caspase-3 in complex with our caspase-specific aza-peptide methyl ketone inhibitor with an aza-Asp residue at P1 revealed a covalent linkage between the inhibitor carbonyl carbon and the active site cysteinyl sulphur. Aza-peptide aldehydes and ketones showed no cross-reactivity towards cathepsin B or chymotrypsin. The initial in vitro selectivity of these inhibitors makes them suitable candidates for further development into therapeutic agents to potentially treat multiple myeloma, neurodegenerative diseases, and parasitic infections.


Assuntos
Aldeídos/farmacologia , Compostos Aza/farmacologia , Desenho de Fármacos , Cetonas/farmacologia , Peptídeos/farmacologia , Inibidores de Proteases/farmacologia , Aldeídos/química , Animais , Compostos Aza/química , Bovinos , Cristalografia por Raios X , Cisteína Endopeptidases/metabolismo , Relação Dose-Resposta a Droga , Humanos , Cetonas/química , Modelos Moleculares , Estrutura Molecular , Peptídeos/química , Inibidores de Proteases/síntese química , Inibidores de Proteases/química , Complexo de Endopeptidases do Proteassoma/metabolismo , Relação Estrutura-Atividade
SELEÇÃO DE REFERÊNCIAS
DETALHE DA PESQUISA
...