Linked Life Data

19751192

Source:http://linkedlifedata.com/resource/pubmed/id/19751192

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
6
pubmed:dateCreated
2009-11-26
pubmed:abstractText
Anionic antimicrobial peptides / proteins (AAMPs) were first reported in the early 1980s and since then, have been established as an important part of the innate immune systems of vertebrates, invertebrates and plants. These peptides are active against bacteria, fungi, viruses and pests such as insects. AAMPs may be induced or expressed constitutively and in some cases, antimicrobial activity appears to be a secondary role for these peptides with other biological activities constituting their primary role. Structural characterization shows AAMPs to generally range in net charge from -1 to -7 and in length from 5 residues to circa 70 residues and for a number of these peptides, post-translational modifications are essential for antimicrobial activity. Membrane interaction appears key to the antimicrobial function of AAMPs and to facilitate these interactions, these peptides generally adopt amphiphilic structures. These architectures vary from the alpha-helical peptides of some amphibians to the cyclic cystine knot structures observed in some plant proteins. Some AAMPs appear to use metal ions to form cationic salt bridges with negatively charged components of microbial membranes, thereby facilitating interaction with their target organisms, but in many cases, the mechanisms underlying the antimicrobial action of these peptides are unclear or have not been elucidated. Here, we present an overview on current research into AAMPs, which suggests that these peptides are an untapped source of putative antimicrobial agents with novel mechanisms of action and possess potential for application in the medical and biotechnological arenas.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
1875-5550
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
585-606
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Anionic antimicrobial peptides from eukaryotic organisms.
pubmed:affiliation
School of Forensic and Investigative Science, University of Central Lancashire Preston PR1 2HE, UK.
pubmed:publicationType
Journal Article, Review