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The Antimicrobial peptide databases may be divided into two categories on the basis of the source of peptides it contains, as specific databases and general databases. These databases have various tools for antimicrobial peptides analysis and prediction. For example, the APD has a widely used calculation interface.
The first structures of these antimicrobial agents were produced by pioneering work by Gross and Morell in the late 1960s and early 1970s, thus marking the formal introduction of lantibiotics. Since then, lantibiotics such as nisin have been used auspiciously for food preservation and have yet to encounter significant bacterial resistance .
The name 'defensin' was coined in the mid-1980s, though the proteins have been called 'Cationic Antimicrobial Proteins,' 'Neutrophil peptides,' 'Gamma thionins' amongst others. [6] Proteins called 'defensins' are not all evolutionarily related to one another. [7] Instead fall into two broad superfamilies, each of which contains multiple families.
n/a n/a Ensembl n/a n/a UniProt n a n/a RefSeq (mRNA) n/a n/a RefSeq (protein) n/a n/a Location (UCSC) n/a n/a PubMed search n/a n/a Wikidata View/Edit Human Cathelicidin antimicrobial peptide (CAMP) is an antimicrobial peptide encoded in the human by the CAMP gene. The active form is LL-37. In humans, CAMP encodes the peptide precursor CAP-18 (18 kDa), which is processed by proteinase 3 ...
Defensins are integral components of the innate immune system and belong to the ancient superfamily of antimicrobial peptides (AMPs). AMPs are also known as host defense peptides (HDPs), [ 2 ] and they are thought to have diverged about 1.4 billion years ago before the evolution of prokaryotes and eukaryotes.
Cecropins are antimicrobial peptides. [1] [2] They were first isolated from the hemolymph of Hyalophora cecropia, whence the term cecropin was derived. Cecropins lyse bacterial cell membranes; they also inhibit proline uptake and cause leaky membranes. Cecropins [3] [4] [5] constitute a main part of the innate immune system of insects.
The beta defensins are antimicrobial peptides implicated in the resistance of epithelial surfaces to microbial colonization. Defensins are 2 to 6 kDa, cationic, microbicidal peptides active against many Gram-negative and Gram-positive bacteria, fungi, and enveloped viruses, [ 1 ] containing three pairs of intramolecular disulfide bonds.
Dermcidin is a protein with 110 amino acids that in humans is encoded by the DCD gene. [3] [4] The full-length protein produces derived peptides as proteolysis-inducing factor (PIF) and other anti-microbial peptides, [4] secreted by human eccrine sweat glands onto the skin as a part of the innate host defense of the immune system.