2jsb: Difference between revisions

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==Overview==

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.

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.

==About this Structure==

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[[Category: Groetzinger, J.]]

[[Category: Hecht, O.]]

[[Category: Jakovkin, I.B.]]

[[Category: Jakovkin, I B.]]

[[Category: Krasnosdembskaya, A.D.]]

[[Category: Krasnosdembskaya, A D.]]

[[Category: Leippe, M.]]

[[Category: antimicrobial]]

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[[Category: poreforming]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:05:36 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-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.
+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.
 ==About this Structure==
@@ Line 16: / Line 16: @@
 [[Category: Groetzinger, J.]]
 [[Category: Hecht, O.]]
-[[Category: Jakovkin, I.B.]]
+[[Category: Jakovkin, I B.]]
-[[Category: Krasnosdembskaya, A.D.]]
+[[Category: Krasnosdembskaya, A D.]]
 [[Category: Leippe, M.]]
 [[Category: antimicrobial]]
@@ Line 28: / Line 28: @@
 [[Category: poreforming]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 13 08:14:02 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:05:36 2008''