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Título: | Creating Diversity in peptide libraries: new customizable units for the site-selective modification of peptides |
Autor: | Boto, Alicia CSIC ORCID | Fecha de publicación: | 5-oct-2014 | Citación: | Peptides in Paris Symposium PIPS (2014) | Resumen: | The modification of peptides has allowed the discovery of new drugs and drug candidates, medical probes, foldamers, peptide catalysts and many other valuable products. In the traditional approach to synthesize peptides, each compound is synthesized de novo, a procedure which is costly in time and materials. Another approach is the site-selective modification of peptides, where one unit can be selectively transformed, while the other units are not affected. Thus, a library of modified peptides can be generated from a single peptide. However, this strategy presents a drawback: if several identical units are present in the peptide, it is difficult to differentiate among them. Recently, we introduced natural and inexpensive 4-hydroxy-L-proline as a customizable unit, which could be converted into a variety of N-alkyl-L-aminoacids The orthogonal protection of its lateral chain allows differentiation of the Hyp units. The advances progress in this work will be commented, including the formation of small branched peptides with medicinal interest. | Descripción: | Trabajo presentado en "Peptides in Paris Symposium PIPS" celebrado en París del 5 al 8 de octubre de 2014. | URI: | http://hdl.handle.net/10261/180979 |
Aparece en las colecciones: | (IPNA) Comunicaciones congresos |
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