Theoretical conformational analysis and synthesis of analogues of the heptapeptide antibiotic K-582 A
| Autor: | Bernard Wathelet, Françoise Demeuse, C. Mayon, J. Brakel, M. Culot, J.L. De Coen |
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| Rok vydání: | 2009 |
| Předmět: |
Models
Molecular Protein Folding Protein Conformation Stereochemistry medicine.drug_class Molecular Sequence Data Antibiotics Peptide Biochemistry Structure-Activity Relationship chemistry.chemical_compound Peptide synthesis medicine Computer Simulation Amino Acid Sequence Protein secondary structure chemistry.chemical_classification Bacteria Computer aid Fungi Anti-Bacterial Agents Solutions Folding (chemistry) chemistry Peptides Antimicrobial Cationic Peptides |
| Zdroj: | International Journal of Peptide and Protein Research. 43:10-18 |
| ISSN: | 0367-8377 |
| DOI: | 10.1111/j.1399-3011.1994.tb00369.x |
| Popis: | A detailed theoretical conformational analysis of the linear heptapeptide antibiotic [Arg2]K-582 A (Arg-Arg-D-Orn-Thr-D-Orn-Lys-D-Tyr) was carried out. The results of the computer simulation suggest that the linear peptide has a high propensity to fold in solution into a quasi-cyclic conformation in equilibrium with pi(L-D) helices. The synthesis of two inactive analogues with an L-Lys in place of D-Orn3 or D-Orn5 confirms the importance of the proposed folding pattern for the occurrence of the antimicrobial activity of K-582 A. |
| Databáze: | OpenAIRE |
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