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1.
Cancer Lett ; 570: 216332, 2023 08 28.
Artigo em Inglês | MEDLINE | ID: mdl-37541540

RESUMO

Cancer poses a significant global health burden, necessitating the widespread use of chemotherapy and radiotherapy as conventional frontline interventions. Although targeted therapy and immunotherapy have shown remarkable advancements, the challenges of resistance development and severe side effects persist in cancer treatment. Consequently, researchers have actively sought more effective alternatives with improved safety profiles. In recent years, curcumin, a natural polyphenolic phytoalexin, has garnered considerable attention due to its broad spectrum of biological effects. This concise review provides valuable insights into the role of curcumin in cancer therapy, with a focus on elucidating its molecular mechanisms in inducing programmed cell death of tumor cells and suppressing tumor cell metastasis potential. Additionally, we discuss the challenges associated with the clinical application of curcumin and explore current endeavors aimed at overcoming these limitations. By shedding light on the promising potential of curcumin, this review contributes to the advancement of cancer treatment strategies.


Assuntos
Curcumina , Neoplasias , Humanos , Curcumina/farmacologia , Curcumina/uso terapêutico , Neoplasias/patologia , Apoptose , Imunoterapia
2.
Food Chem ; 342: 128212, 2021 Apr 16.
Artigo em Inglês | MEDLINE | ID: mdl-33069539

RESUMO

The current study focused on the investigation of laccase-catalyzed conjugation of potato protein (PPT) with selected pectic polysaccharides (PPS) and modulation of the conjugation in order to obtain desired functional ingredients. PPS, including sugar beet pectin/arabinan, apple/citrus pectin and potato galactan, were evaluated as substrates in the conjugation reaction-catalyzed by laccases (Trametes versicolor-LacTv, Coriolus hirsutus-LacCh). LacCh exhibited a higher catalytic efficiency than LacTv. The reactivity of PPT/PPS and their ratio were determinants for their heteroconjugation. Both laccases exhibited the highest specificity towards the conjugation of PPT/sugar beet pectin. Predictive models were developed for conjugation efficiency and emulsification performance. The conjugation extent was negatively affected by the protein proportion and the protein proportion/enzyme concentration interaction; while the emulsification performance was positively correlated with the protein proportion and the protein proportion/reaction time interaction. This study contributed to the understanding of laccase-catalyzed conjugation reaction for the controlled synthesis of conjugated-PTT as functional ingredients.


Assuntos
Emulsões/química , Lacase/metabolismo , Proteínas de Plantas/metabolismo , Polissacarídeos/química , Solanum tuberosum/metabolismo , Biocatálise , Oxirredução , Tamanho da Partícula , Pectinas/química , Pectinas/metabolismo , Proteínas de Plantas/química , Polissacarídeos/metabolismo , Análise de Regressão , Solubilidade
3.
Enzyme Microb Technol ; 143: 109694, 2021 Feb.
Artigo em Inglês | MEDLINE | ID: mdl-33375965

RESUMO

Laccase can catalyze the oxidative cross-linking of peptides, which is useful in the production of proteinaceous materials with enhanced functional properties. However, the kinetics and the pathway of this reaction remain unclear. In the present study, laccase-catalyzed oxidative cross-linking reaction was investigated through a combination of computational analysis, kinetic studies and end-product profiling using selected substrate models, including peptide AG-10 (AKKIVSDGNG) (without tyrosine) derived from lysozyme and tyrosine-containing peptide ST-10 (SYMTDYYLST) from potato protein (patatin), and tyrosine. Both laccases from Trametes versicolor (LacTv) and Coriolus hirsutus (LacCh) were used as biocatalysts. Laccase exhibited higher binding affinity and catalytic efficiency (kcat/Km) towards ST-10 and AG-10 than tyrosine. Among the laccases, LacCh showed higher kcat towards the substrate models than LacTv. Through the molecular docking, this result was attributed to the presence of the ASN206 at the cavity of LacCh. The end product profiles reveal the formation of homo-oligomers (> 5 units) of ST-10 in the reaction catalyzed by LacTv, while polymerization was favored by LacCh. These cross-linked products were identified to have a mix of oligo-tyrosine linkages. In contrast, the cross-linking of AG-10 required the presence of ferulic acid as mediator, which resulted in the formation of hetero-oligomers and polymers of AG-10. The knowledge obtained in the present study provide insight into an effective reaction for peptide cross-linking.


Assuntos
Lacase , Solanum tuberosum , Catálise , Cinética , Lacase/metabolismo , Simulação de Acoplamento Molecular , Muramidase , Estresse Oxidativo , Peptídeos , Polyporaceae , Trametes/metabolismo , Tirosina
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