Detalle de: Gramicidin S derivatives containing cis- and trans-morpholine amino acids (MAAS) as turn mimetics
| Title | Gramicidin S derivatives containing cis- and trans-morpholine amino acids (MAAS) as turn mimetics |
| Abstract |
The cyclic decapeptide gramicidin S (GS) was used as a model for the evaluation of four turn mimetics. For this purpose, one of the D ‐Phe‐Pro two‐residue turn motifs in the rigid cyclic β‐hairpin structure of GS was replaced with morpholine amino acids (MAA 2 – 5 ), differing in stereochemistry and length of the side‐chain. The conformational properties of the thus obtained GS analogues ( 6 – 9 ) was assessed by using NMR spectroscopy and X‐ray crystallography, and correlated with their biological properties (antimicrobial and hemolytic activity). We show that compound 8 , containing the dipeptide isostere trans ‐MAA 4 , has an apparent high structural resemblance with GS and that its antibacterial activity against a panel of Gram positive and ‐negative bacterial strains is better than the derivatives 6 , 7 and 9 . |
| Apa Reference | Kapoerchan, V. V., Spalburg, E., de Neeling, Albert. J., Mars‐Groenendijk, R. H., Noort, D., Otero, J. M., Ferraces‐Casais, P., Llamas‐Saiz, A. L., van Raaij, M. J., van Doorn, J., van der Marel, G. A., Overkleeft, H. S., & Overhand, M. (2010). Gramicidin S Derivatives Containing cis‐ and trans‐Morpholine Amino Acids (MAAs) as Turn Mimetics. Chemistry – A European Journal, 16(14), 4259–4265. Portico. 10.1002/chem.200902984 |
| Doi | 10.1002/chem.200902984 |
| Publication Date | Apr 2010 |
| Publication Type | Article |
| Researcher | Mark van Raaij |
| Ontology | Experimental structure determination, Molecular flexibility, Sequence analysis |
| Research Groups | Structural Biology of Virus Proteins |
| Tools |