Activity of Cathelicidin Peptides against Simkania negevensis
| Autor: | Paola Nardini, Roberto Cevenini, Antonietta Di Francesco, N. Fiani, Monica Benincasa, Maria Di Paolo, Manuela Donati, Renato Gennaro, Claudio Foschi |
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| Přispěvatelé: | Donati, M., Di Francesco, A., Di Paolo, M., Fiani, N., Benincasa, Monica, Gennaro, Renato, Nardini, P., Foschi, C., Cevenini, R., Donati M., Di Francesco A., Di Paolo M., Fiani N., Benincasa M., Gennaro R., Cardini P., Foschi C., Cevenini R. |
| Jazyk: | angličtina |
| Rok vydání: | 2011 |
| Předmět: |
antimicrobial peptide
Article Subject medicine.medical_treatment cathelicidin Simkania negevensis antimicrobial peptides PMAP-37 amphipathic helix myeloid cells Antimicrobial peptides Chlamydiae Bioinformatics Biochemistry Microbiology Cathelicidin medicine Volume concentration biology Strain (chemistry) business.industry biology.organism_classification In vitro Cathelicidins Simkania negevensi lipids (amino acids peptides and proteins) business Research Article |
| Zdroj: | International Journal of Peptides |
| ISSN: | 1687-9767 |
| DOI: | 10.1155/2011/708710 |
| Popis: | A molecular biological approach, based on preproregion homology in the precursors of several diverse antibacterial peptides, was used to clone a pig bone marrow cDNA encoding a novel 167-residue polypeptide. The preproregion of this polypeptide is highly similar to corresponding regions in congeners from pig, cattle and rabbit. It is followed by a unique, cationic, 37-residue sequence, which was predicted to have a high propensity for an α-helical conformation. A peptide, termed PMAP-37, corresponding to this sequence, was chemically synthesized and shown to undergo a transition from a random coil to an ordered, mainly helical, conformation on addition of trifluoroethanol. This behaviour is typical of an amphipathic α helix, a structure common to several membrane-active, antimicrobial peptides. In vitro experiments showed that PMAP-37 strongly inhibits the growth of several strains of Gram-negative and Gram-positive bacteria, with minimal inhibitory concentrations ranging over 1–4 μM, and permeabilizes the inner membrane of Escherichia coll. Interestingly, the 15–32 stretch of PMAP-37 show a remarkable similarity to N-terminal stretches in cecropins B and A from Drosophila melanogaster and Cecropia hyalophora, respectively. This affords an uncommon example of sequence convergence. |
| Databáze: | OpenAIRE |
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