2jni: Difference between revisions

Arenicins are 21-residue cationic antimicrobial peptides, isolated from marine polychaeta Arenicola marina. In order to determine a high-resolution three-dimensional structure of arenicin-2, the recombinant peptide was overexpressed as a fused form in Escherichia coli. Both arenicin isoforms were synthesized using the Fmoc-based solid-phase strategy. Recombinant and synthetic arenicins were purified, and their antimicrobial and spectroscopic properties were analyzed. NMR investigation shows that in water solution arenicin-2 displays a prolonged beta-hairpin, formed by two antiparallel beta-strands and stabilized by one disulfide and nine hydrogen bonds. A significant right-handed twist in the beta-sheet is deprived the peptide surface of amphipathicity. CD spectroscopic analysis indicates that arenicin-2 binds to the SDS and DPC micelles, and conformation of the peptide is significantly changed upon binding. Arenicin strongly binds to anionic lipid (POPE/POPG) vesicles in contrast with zwitterionic (POPC) ones. These results suggest that arenicins are membrane active peptides and point to possible mechanism of their selectivity toward bacterial cells.

[[Category: Arseniev, A S.]]

[[Category: Balandin, S V.]]

[[Category: Finkina, E I.]]

[[Category: Kokryakov, V N.]]

[[Category: Kudelina, I A.]]

[[Category: Nadezhdin, K D.]]

[[Category: Ovchinnikova, T V.]]

[[Category: Shenkarev, Z O.]]

[[Category: Zhmak, M N.]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:04:25 2008''