Video Experimental Relacionado
Updated: Jun 18, 2025
09:34
Synthesis of Information-bearing Peptoids and their Sequence-directed Dynamic Covalent Self-assembly
Published on: February 6, 2020
7.2K
Control alostérico de las propiedades catalíticas de los conjuntos supramoleculares basados en dipeptídios
Soumili Roy1, Janmejay Laha1, Antara Reja1
1Department of Chemical Sciences and Centre for Advanced Functional Materials, Indian Institute of Science Education and Research (IISER) Kolkata, Mohanpur 741246, India.
Journal of the American Chemical Society
|August 1, 2024
Resumen
Los investigadores diseñaron un catalizador mínimo utilizando un dipeptídeo que forma agregados para las reacciones. Este catalizador
Área de la Ciencia:
- Biología Química
- Química supramolecular
- Catálisis
Sus antecedentes:
- Allostery regula la actividad biológica a través de cambios conformacionales en la unión del efector.
- La regulación de las enzimas es crucial para controlar las vías bioquímicas.
- Los diseños minimalistas ofrecen información sobre los principios fundamentales del reconocimiento molecular y la catálisis.
Objetivo del estudio:
- Para demostrar un diseño de catalizador alostérico mínimo utilizando un dipeptido.
- Para investigar el autoensamblaje de los estados activos catalíticos.
- Para explorar el control temporal sobre la actividad catalítica a través de redes de retroalimentación.
Principales métodos:
- La condensación del dipeptido con aldehídos para formar agregados esféricos.
- Aprovechamiento del enlace inmine dinámico para el autoensamblaje.
- Utilizando el grupo amino como un sitio alostérico para la unión al inhibidor.
- Implementación de redes de reacción autónomas controladas por retroalimentación.
Principales resultados:
- Se diseñó un catalizador mínimo basado en dipeptídeos, formando agregados esféricos catalíticamente activos.
- La inhibición alostérica se logró a través de la unión del inhibidor al sitio de la amina, regulando a la baja la actividad catalítica.
- Se demostró el control temporal de la actividad del catalizador utilizando un bucle de retroalimentación y la actividad hidrolítica.
Conclusiones:
- Se diseñó y demostró con éxito un catalizador alostérico de autoensamblaje mínimo.
- El sistema exhibe actividad catalítica sintonizable a través de la regulación alostérica y el control temporal.
- Este trabajo proporciona una base para el desarrollo de sistemas catalíticos dinámicos y sensibles.
Videos de Conceptos Relacionados
01:58Cooperative Allosteric Transitions
7.9K
Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
7.9K
01:19Allosteric Proteins-ATCase
5.7K
Binding sites linkages can regulate a protein's function. For example, enzyme activity is often regulated through a feedback mechanism where the end product of the biochemical process serves as an inhibitor.
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
Aspartate transcarbamoylase (ATCase) is a cytosolic enzyme that catalyzes the condensation of L-aspartate and carbamoyl phosphate to N-carbamoyl-L-aspartate. This reaction is the first step in pyrimidine biosynthesis. UTP and CTP, the end products of the pyrimidine synthesis...
5.7K
01:08Allosteric Regulation
57.8K
Allosteric regulation of enzymes occurs when the binding of an effector molecule to a site that is different from the active site causes a change in the enzymatic activity. This alternate site is called an allosteric site, and an enzyme can contain more than one of these sites. Allosteric regulation can either be positive or negative, resulting in an increase or decrease in enzyme activity. Most enzymes that display allosteric regulation are metabolic enzymes involved in the degradation or...
57.8K
00:49Ligand Binding and Linkage
4.8K
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked. In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
4.8K
02:40Ligand Binding Sites
12.8K
Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
12.8K
01:13Introduction to Mechanisms of Enzyme Catalysis
8.0K
For many years, scientists thought that enzyme-substrate binding took place in a simple "lock-and-key" fashion. This model stated that the enzyme and substrate fit together perfectly in one instantaneous step. However, current research supports a more refined view scientists call induced fit. The induced-fit model expands upon the lock-and-key model by describing a more dynamic interaction between enzyme and substrate. As the enzyme and substrate come together, their interaction causes...
8.0K