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Oligo-benzamide-based peptide mimicking tools for modulating biology.
Chen, Chia-Yuan; Elmore, Scott; Lalami, Ismail; Neal, Henry; Vadlamudi, Ratna K; Raj, Ganesh V; Ahn, Jung-Mo.
Afiliación
  • Chen CY; Department of Chemistry and Biochemistry, University of Texas at Dallas, Richardson, TX, United States.
  • Elmore S; Department of Chemistry and Biochemistry, University of Texas at Dallas, Richardson, TX, United States.
  • Lalami I; Department of Chemistry and Biochemistry, University of Texas at Dallas, Richardson, TX, United States.
  • Neal H; Department of Chemistry and Biochemistry, University of Texas at Dallas, Richardson, TX, United States.
  • Vadlamudi RK; Department of Obstetrics and Gynecology, University of Texas Health Science Center at San Antonio, San Antonio, TX, United States.
  • Raj GV; Department of Urology, University of Texas Southwestern Medical Center, Dallas, TX, United States.
  • Ahn JM; Department of Chemistry and Biochemistry, University of Texas at Dallas, Richardson, TX, United States. Electronic address: jungmo.ahn@utdallas.edu.
Methods Enzymol ; 698: 221-245, 2024.
Article en En | MEDLINE | ID: mdl-38886033
ABSTRACT
The oligo-benzamide scaffold is a rigid organic framework that can hold 2-3 functional groups as O-alkyl substituents on its benzamide units, mirroring their natural arrangement in an α-helix. Oligo-benzamides demonstrated outstanding α-helix mimicry and can be readily synthesized by following high yielding and iterative reaction steps in both solution-phase and solid-phase. A number of oligo-benzamides have been designed to emulate α-helical peptide segments in biologically active proteins and showed strong protein binding, in turn effectively disrupting protein-protein interactions in vitro and in vivo. In this chapter, the design of oligo-benzamides for mimicking α-helices, efficient synthetic routes for producing them, and their biomedical studies showing remarkable potency in inhibiting protein functions are discussed.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Benzamidas Límite: Animals / Humans Idioma: En Revista: Methods Enzymol Año: 2024 Tipo del documento: Article Pais de publicación: Estados Unidos
Texto completo
Añadir a Mi BVS
Imprimir
XML
PubMed Links
Buscar en Google

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Benzamidas Límite: Animals / Humans Idioma: En Revista: Methods Enzymol Año: 2024 Tipo del documento: Article Pais de publicación: Estados Unidos