Linked Life Data

12044162

Source:http://linkedlifedata.com/resource/pubmed/id/12044162

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
23
pubmed:dateCreated
2002-6-4
pubmed:abstractText
Animal-derived antimicrobial peptides are gaining increasing interest for their role in the innate immune system and for their potential applications in the antimicrobial field. Defining the factors that affect potency and selectivity is presently a major challenge to their effective and safe use. Since amidating the C-terminal carboxyl is one of the means of enhancing antimicrobial activity, we report here our comparative study of the solution structures of the antimicrobial peptide dermaseptin S3 and its amidated analogue. Circular dichroism measurements suggested that the peptides are basically found in an alpha-helical structure. In contrast, NMR measurements revealed the complete absence of alpha-helical elements in S3 and a single four-residue helix in the amidated analogue. Whereas the native peptide was found to be flexible, containing a hydrogen-bonded turn and bends, the amidated analogue exhibited a defined alpha-helix at the C-terminal region, causing the latter to be significantly elongated and more structured. Hence, although the increased potency in amidated antimicrobial peptides can be attributed to the increased overall positive charge, in this case, amidation has had additional effects beyond modifying the net positive charge. It has induced and/or stabilized a helical conformation, causing the amidated dermaseptin to be more rigid and more extended than its nonamidated analogue. The possible implications on the mode of action are discussed herein.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
11
pubmed:volume
41
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7312-7
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2002
pubmed:articleTitle
Structural consequences of carboxyamidation of dermaseptin S3.
pubmed:affiliation
The Wolfson Centre for Applied Structural Biology, Hebrew University of Jerusalem, Safra Campus, Givat Ram, 91904 Jerusalem, Israel.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't