Research Article

Towards Identify Selective Antibacterial Peptides Based on Abstracts Meaning

Box 1

One example of a pattern abstract.
(1)  Biochem Biophys Res Commun.
2006 Sep 22;348(2):514-23.
Epub 2006 Jul 28.
Aurelin, a novel antimicrobial peptide
from jellyfish Aurelia aurita with
structural features of defensins
and channel-blocking toxins.
Ovchinnikova TV, Balandin SV, Aleshina
GM, Tagaev AA, Leonova YF, Krasnodembsky
ED, Men’shenin AV, Kokryakov VN.
Shemyakin and Ovchinnikov Institute of
Bioorganic Chemistry, Russian Academy of
Sciences, Miklukho-Maklaya str. 16/10,
117997 Moscow, Russia. [email protected]
A novel 40-residue antimicrobial peptide,
aurelin, exhibiting activity against
Gram-positive and Gram-negative bacteria,
was purified from the mesoglea of a
scyphoid jellyfish Aurelia aurita by
preparative gel electrophoresis and RP-HPLC.
Molecular mass (4296.95Da) and complete
amino acid sequence of aurelin
(AACSDRAHGHICESFKSFCKDSGRNGVKLRANCKKTCGLC)
were determined. Aurelin has six
cysteines forming three disulfide bonds.
The total RNA was isolated from the
jellyfish mesoglea, RT-PCR and cloning
were performed, and cDNA was sequenced.
A 84-residue preproaurelin contains a
putative signal peptide (22 amino acids) and
a propiece of the same size (22 amino acids).
Aurelin has no structural homology with any
previously identified antimicrobial peptides
but reveals partial similarity both with
defensins and K+ channel-blocking toxins
of sea anemones and
belongs to ShKT domain family.
PMID: 16890198 [PubMed -indexed for MEDLINE]