title: 3-Substituted prolines: from synthesis to structural applications, from peptides to foldamers.
abstract: 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 b-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.
authors: Laboratoire des BioMolécules, Université Pierre et Marie Curie-Sorbonne Universités, UMR 7203 and FR 2769, Paris 75005, France.
authors: Céline
authors: C
authors: Mothes
authors: Cécile
authors: C
authors: Caumes
authors: Alexandre
authors: A
authors: Guez
authors: Héloïse
authors: H
authors: Boullet
authors: Thomas
authors: T
authors: Gendrineau
authors: Sylvain
authors: S
authors: Darses
authors: Nicolas
authors: N
authors: Delsuc
authors: Roba
authors: R
authors: Moumné
authors: Benoit
authors: B
authors: Oswald
authors: Olivier
authors: O
authors: Lequin
authors: Philippe
authors: P
authors: Karoyan
mesh_terms: D010455:Peptides / Q000737:chemistry*; D011392:Proline / Q000031:analogs & derivatives / Q000138:chemical synthesis* / Q000737:chemistry*; D017433:Protein Structure, Secondary
chemical_list: D010455:Peptides; D011392:Proline