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- W2069970612 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." @default.
- W2069970612 created "2016-06-24" @default.
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- W2069970612 date "2013-02-19" @default.
- W2069970612 modified "2023-10-17" @default.
- W2069970612 title "3-Substituted Prolines: From Synthesis to Structural Applications, from Peptides to Foldamers" @default.
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- W2069970612 doi "https://doi.org/10.3390/molecules18022307" @default.
- W2069970612 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6270394" @default.
- W2069970612 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/23429346" @default.
- W2069970612 hasPublicationYear "2013" @default.
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