Structural highlights
Function
[ANN1_AREMA] Has antimicrobial activity against the Gram-negative bacteria E.coli and P.mirabilis, the Gram-positive bacterium L.monocytogenes and the yeast C.albicans.[1] [2]
Publication Abstract from PubMed
The solution structure and the mode of action of arenicin isoform 1, an antimicrobial peptide with a unique 18-residue loop structure, from the lugworm Arenicola marina were elucidated here. Arenicin folds into a two-stranded antiparallel beta-sheet. It exhibits high antibacterial activity at 37 and 4 degrees C against Gram-negative bacteria, including polymyxin B-resistant Proteus mirabilis. Bacterial killing occurs within minutes and is accompanied by membrane permeabilization, membrane detachment and release of cytoplasm. Interaction of arenicin with reconstituted membranes that mimic the lipopolysaccharide-containing outer membrane or the phospholipid-containing plasma membrane of Gram-negative bacteria exhibited no pronounced lipid specificity. Arenicin-induced current fluctuations in planar lipid bilayers correspond to the formation of short-lived heterogeneously structured lesions. Our results strongly suggest that membrane interaction plays a pivotal role in the antibacterial activity of arenicin.
Structure and mode of action of the antimicrobial peptide arenicin.,Andra J, Jakovkin I, Grotzinger J, Hecht O, Krasnosdembskaya AD, Goldmann T, Gutsmann T, Leippe M Biochem J. 2008 Feb 15;410(1):113-22. PMID:17935487[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Ovchinnikova TV, Aleshina GM, Balandin SV, Krasnosdembskaya AD, Markelov ML, Frolova EI, Leonova YF, Tagaev AA, Krasnodembsky EG, Kokryakov VN. Purification and primary structure of two isoforms of arenicin, a novel antimicrobial peptide from marine polychaeta Arenicola marina. FEBS Lett. 2004 Nov 5;577(1-2):209-14. PMID:15527787 doi:http://dx.doi.org/10.1016/j.febslet.2004.10.012
- ↑ Andra J, Jakovkin I, Grotzinger J, Hecht O, Krasnosdembskaya AD, Goldmann T, Gutsmann T, Leippe M. Structure and mode of action of the antimicrobial peptide arenicin. Biochem J. 2008 Feb 15;410(1):113-22. PMID:17935487 doi:http://dx.doi.org/BJ20071051
- ↑ Andra J, Jakovkin I, Grotzinger J, Hecht O, Krasnosdembskaya AD, Goldmann T, Gutsmann T, Leippe M. Structure and mode of action of the antimicrobial peptide arenicin. Biochem J. 2008 Feb 15;410(1):113-22. PMID:17935487 doi:http://dx.doi.org/BJ20071051
