Metallacyclopeptide

Therefore, linear peptides with two metal binding sites were obtained by solid phase synthesis. Upon coordination of these ligands to a metal centre a metalla-cyclopeptide will be formed. The choosen peptide sequences are found in naturally occuring proteins or cyclopeptides, which bioactivities depends on the sequence of the amino acids as well as it´s loop type structure. Pd(II) and Mo(VI)O2 are used as metal centres to obtain different conformations at the peptide backbone in the metalla-cyclopeptides. This requires the use of pyridine and catechol as metal binding sites. Following to this concept, a series of Mo(VI)O2-metalla-cyclopeptides could be obtained in a highly stereoselektiv manner. These metalla-cyclopeptides represents analogs of the RGD front in Echistatin, which binds to the integrins, of the estrogen-like cyclopeptides Segetalin A and B and finally of the somatostatin-like cyclopeptide Urotensin II, which posses vasoconstrictor activity. Furthermore, pentapeptide-bridged macrocyclic Mo(VI)O2-complexes were synthesized, that offers more knowledge in the stabilisation of peptide-a-helical structure.

Grantor dc:publisher

Publikationsserver der RWTH Aachen University

Year dc:date

2004

Author dc:creator

• Stortz, Patrick

Contributors dc:contributor

• Albrecht, Markus

• info:eu-repo/classification/ddc/540
• Übergangsmetallkomplexe
• Cyclopeptide
• Makrocyclische Verbindungen
• Chemie
• Metallkoordination
• Festphasensynthese

Statement dc:rights

• info:eu-repo/semantics/openAccess

Language dc:language

ger

Identifier

https://publications.rwth-aachen.de/search?p=id:%22RWTH-CONV-114925%22

OAI record oai:identifier

https://publications.rwth-aachen.de/oai2d?verb=GetRecord&metadataPrefix=oai_dc&identifier=oai%3Apublications.rwth-aachen.de%3A52723