Pharmaceutical applications of peptidomimetics

Autor:	Michael G. Kahn, Maher Qabar, Charles Sia, Michèl R. Klein, Jan Urban
Rok vydání:	1996
Předmět:	chemistry.chemical_classification Functional diversity Solid-phase synthesis Biochemistry chemistry Peptidomimetic Pharmacology toxicology Native protein Protein secondary structure Amino acid
Zdroj:	Letters in Peptide Science. 3:25-30
ISSN:	1573-496X 0929-5666
Popis:	Nature has used a ‘library approach’ to constructing ligands for specific receptors and enzymes by combining a limited functional diversity of 20 amino acid side chains with a small array of secondary structure motifs — reverse turns, α-helices and β-strands. The dissection of multidomain proteins into small synthetic conformationally restricted components is an important step in the design of low-molecular-weight nonpeptides that mimic the activity of the native protein. Mimetics of critical functional domains might possess beneficial properties with regard to specificity and therapeutic potential compared to the intact proteinaceous species. Combinatorial secondary-structure-templated libraries provide a powerful engine for the development of novel vaccines and pharmaceuticals.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::3039b5ac5b2773279b02aa3c7d9c26e3 https://doi.org/10.1007/bf00131082 Zobrazit plný text záznamu Full text from SpringerLink