Conformation of cyclic peptides. Principle concepts and the design of selectivity and superactivity in bioactive sequences by 'spatial screening'

H. Kessler, R. Gratias, G. Hessler, M. Gurrath, G. Müller

Research output: Contribution to journalArticlepeer-review

83 Scopus citations

Abstract

The description of small cyclic peptide conformations can be simplified by substitution of the peptide bond for an olefinic structure, which then is converted into a single bond (for the E configuration) or a pseudo-CH2-group (for Z olefins). The resulting cycloalkane conformations are related to the observed cyclic peptide structures. The individual conformation, however, is strongly influenced by the array of chirality in the peptide sequence. This can be used for a "spatial screening" of biologically active peptide sequences. The procedure is demonstrated on selective and highly active inhibitors for αvβ3 integrins with a strong potential for development into anticancer drugs.

Original languageEnglish
Pages (from-to)1201-1205
Number of pages5
JournalPure and Applied Chemistry
Volume68
Issue number6
DOIs
StatePublished - Jun 1996

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