The crystal structures of the synthetic C-terminal octa- and dodecapeptides of trichovirin
✍ Scribed by Renate Geßmann; Panaiotis Benos; Hans Brückner; Michael Kokkinidis
- Publisher
- John Wiley and Sons
- Year
- 1999
- Tongue
- English
- Weight
- 187 KB
- Volume
- 5
- Category
- Article
- ISSN
- 1075-2617
No coin nor oath required. For personal study only.
✦ Synopsis
The structures of two synthetic peptides with sequences corresponding to the C-terminal region of the naturally occurring 14-residue peptaibol trichovirin have been determined. The crystal structures of 8and 12-residue segments are presented and are compared with the structures of the tetrapeptide and of the 9-residue segment, which have been reported earlier. A comparison between these segments leads to the hypothesis that the three-dimensional structure of trichovirin is to a large extent determined by the properties of a periodically repeating -Aib-Pro-pattern in the sequence of the peptide.
📜 SIMILAR VOLUMES
The dodecapepetide sequence R-L-C-R-I-V-V-I-R-V-C-R with a disulfide bridge between the cysteine residues found in bovine neutrophils was synthesized by solid-phase procedures. Its antimicrobial activity against oral microorganisms such as Actinobacillus actinomycetemcomitans, Porphyromonas gingival
Pathological changes in the microtubule associated protein tau, leading to tau-containing filamentous lesions, are a major hallmark common to many types of human neurodegenerative diseases, including Alzheimer's disease (AD). No structural data are available which could rationalize the extensive con