Structurally Selective Assembly of a Specific Macrobicycle From a Dynamic Library of Pseudopeptidic Disulfides
Molecular recognition is essential in many chemical and biological processes. Studying the behavior of pseudopeptides using dynamic covalent chemistry allows the exploration of a wide range of structural components and molecular interactions with minimal synthetic effort. Herein, we describe how non...
| Autores: | , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión aceptada para publicación |
| Fecha de publicación: | 2019 |
| País: | España |
| Institución: | Consejo Superior de Investigaciones Científicas (CSIC) |
| Repositorio: | DIGITAL.CSIC. Repositorio Institucional del CSIC |
| OAI Identifier: | oai:digital.csic.es:10261/179334 |
| Acceso en línea: | http://hdl.handle.net/10261/179334 |
| Access Level: | acceso abierto |
| Palabra clave: | Topology Peptidomimetics Self-assembly Noncovalent interactions |
| Sumario: | Molecular recognition is essential in many chemical and biological processes. Studying the behavior of pseudopeptides using dynamic covalent chemistry allows the exploration of a wide range of structural components and molecular interactions with minimal synthetic effort. Herein, we describe how non‐covalent attractive forces in pseudopeptidic building blocks can successfully guide the product distribution in a dynamic library towards topologically more complex compounds that are in principle not expected. The interactions described herein are highly dependent on molecular architecture and media so effective recognition can be altered by just minimal structural or environmental changes. Thus, the chemical and constitutional information contained in the respective building blocks is decoded and expressed through dynamic covalent and non‐covalent bonds in the assembly of either a single macrostructure or an ensemble of components with larger structural diversity. The understanding of supramolecular forces responsible for the component assembly in minimalistic systems can help to comprehend more complex bio‐related processes such as protein folding or protein−protein interactions. |
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