相关实验视频

Updated: Jun 13, 2025

Covalent Fragment Screening Using the Quantitative Irreversible Tethering Assay
06:17

Covalent Fragment Screening Using the Quantitative Irreversible Tethering Assay

Published on: February 28, 2025

470

基于triazole的针对性共价抑制剂cruzipain的结构辅助计算设计

Juan Pablo Cerutti1,2, Lucas Abreu Diniz3, Viviane Corrêa Santos3

  • 1Unidad de Investigación y Desarrollo en Tecnología Farmacéutica (UNITEFA-CONICET), Facultad de Ciencias Químicas, Universidad Nacional de Córdoba (FCQ-UNC), Haya de la Torre y Medina Allende, Córdoba 5000, Argentina.

Molecules (Basel, Switzerland)
|September 14, 2024
PubMed
概括

研究人员开发了新的三醇化合物,其向的是沙加斯病的关键酶cruzipain (CZP). 一种化合物,Ald-6,表现出强大的抗寄生虫活性和低毒性,使其成为进一步药物开发的有希望的候选者.

关键词:
查加斯病是查加斯病的一种疾病.克鲁兹帕因 (Cruzipain) 是一种疼痛.计算机辅助药物设计有针对性的共价抑制剂.三醇衍生物的三醇衍生物

更多相关视频

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules10:58

Protein WISDOM: A Workbench for In silico De novo Design of BioMolecules

Published on: July 25, 2013

17.0K
Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors10:33

Development of Inhibitors of Protein-protein Interactions through REPLACE: Application to the Design and Development Non-ATP Competitive CDK Inhibitors

Published on: October 26, 2015

11.3K

相关概念视频

Structure-Activity Relationships and Drug Design01:28

Structure-Activity Relationships and Drug Design

Drug design is a dynamic field that involves discovering and developing new medications based on specific biological targets. This process heavily relies on structure-activity relationships (SAR) and quantitative structure-activity relationships (QSAR) to guide the design and optimization of efficient drugs.
SAR studies the intricate relationship between a drug's chemical structure and biological activity. It focuses on understanding how modifications to a drug's structure can influence...
677
Protein-protein Interfaces02:04

Protein-protein Interfaces

Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
12.5K