3-Substituted Prolines: From Synthesis to Structural Applications, from Peptides to Foldamers †

Molecules

Céline Mothes²  Cຜile Caumes²  Alexandre Guez²  Héloïse Boullet²  Thomas Gendrineau¹  Sylvain Darses¹  Nicolas Delsuc²  Roba Moumné²  Benoit Oswald³  Olivier Lequin² 

[1] Laboratoire Charles Friedel, Ecole Normale Supérieure de Chimie de Paris, UMR 7223, 11 rue Pierre et Marie Curie, Paris, 75005, France;Laboratoire des BioMolécules, Université Pierre et Marie Curie-Sorbonne Universités, UMR 7203 and FR 2769, Paris, 75005, France;Genzyme Pharmaceuticals, Eichenweg 1, CH-4410 Liestal, Switzerland

关键词: substituted proline;    peptide;    peptidomimetics;    β-turn;    PPII helix;   

DOI  :  10.3390/molecules18022307

来源: mdpi

【 摘 要 】

Among the twenty natural proteinogenic amino acids, proline is unique as its secondary amine forms a tertiary amide when incorporated into biopolymers, thus preventing hydrogen bond formation. Despite the lack of hydrogen bonds and thanks to conformational restriction of flexibility linked to the pyrrolidine ring, proline is able to stabilize peptide secondary structures such as β-turns or polyproline helices. These unique conformational properties have aroused a great interest in the development of proline analogues. Among them, proline chimeras are tools combining the proline restriction of flexibility together with the information brought by natural amino acids side chains. This review will focus on the chemical syntheses of 3-substituted proline chimeras of potential use for peptide syntheses and as potential use as tools for SAR studies of biologically active peptides and the development of secondary structure mimetics. Their influence on peptide structure will be briefly described.

【 授权许可】

CC BY   
© 2013 by the authors; licensee MDPI, Basel, Switzerland.