Abstract
Substituted proline derivatives represent an important class of conformationally constrained amino acids. The combination of the structural properties of proline and the side-chain of another amino acid could help the development of peptidomimetics and SAR study of active compounds. The presence of a phenyl or a p-hydroxy-phenyl ring on the pyrrolidine ring could be considered as phenylalanine- or thyrosine-proline hybrids. These compounds have shown the potential to mimic natural occurring peptides and can activate or inhibit the respective receptor. This review will focus on the chemical strategy applied to synthesize these analogues.
Keywords: Phenylalanine-proline, tyrosine-proline, amino acid chimeras, constrained amino acid, peptidomimetic.
Current Bioactive Compounds
Title:Synthetic Approach to Phenylalanine-Proline, and Tyrosine-Proline Hybrid Amino Acids
Volume: 12 Issue: 3
Author(s): Marialuigia Fantacuzzi, Letizia Giampietro and Marilena Crescente
Affiliation:
Keywords: Phenylalanine-proline, tyrosine-proline, amino acid chimeras, constrained amino acid, peptidomimetic.
Abstract: Substituted proline derivatives represent an important class of conformationally constrained amino acids. The combination of the structural properties of proline and the side-chain of another amino acid could help the development of peptidomimetics and SAR study of active compounds. The presence of a phenyl or a p-hydroxy-phenyl ring on the pyrrolidine ring could be considered as phenylalanine- or thyrosine-proline hybrids. These compounds have shown the potential to mimic natural occurring peptides and can activate or inhibit the respective receptor. This review will focus on the chemical strategy applied to synthesize these analogues.
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Cite this article as:
Fantacuzzi Marialuigia, Giampietro Letizia and Crescente Marilena, Synthetic Approach to Phenylalanine-Proline, and Tyrosine-Proline Hybrid Amino Acids, Current Bioactive Compounds 2016; 12 (3) . https://dx.doi.org/10.2174/1573407212666160511161243
DOI https://dx.doi.org/10.2174/1573407212666160511161243 |
Print ISSN 1573-4072 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-6646 |
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