Identification of a Novel Antimicrobial Peptide from Brazilian Coast Coral Phyllogorgia dilatata

被引:1
|
作者
de Lima, Loiane Alves [1 ]
Migliolo, Ludovico [1 ]
Barreiro e Castro, Clovis [2 ]
Pires, Debora de Oliveira [2 ]
Lopez-Abarrategui, Carlos [3 ]
Goncalves, Eveline Ferreira [1 ]
Vasconcelos, Ilka Maria [4 ]
Abreu de Oliveira, Jose Tadeu [4 ]
Otero-Gonzalez, Anselmo de Jesus [3 ]
Franco, Octavio Luiz [1 ]
Dias, Simoni Campos [1 ]
机构
[1] Univ Catolica Brasilia, Ctr Anal Prote & Bioquim, Programa Posgrad Ciencias Genom & Biotecnol, Asa Norte, Brazil
[2] Univ Fed Rio de Janeiro, Dept Invertebrados, Museu Nacl, Rio De Janeiro, Brazil
[3] Univ Havana, Fac Biol, Ctr Prot Studies, Lab Inmunoanal & Peptidos Antimicrobianos, Havana, Cuba
[4] Univ Fed Ceara, Dept Bioquim & Biol Mol, Fortaleza, Ceara, Brazil
来源
PROTEIN AND PEPTIDE LETTERS | 2013年 / 20卷 / 10期
关键词
Reef coral; Phyllogorgia dilatata; peptides; human pathogenic bacteria; SEA-URCHIN; HEMOCYTES; PURIFICATION; TUNICATE;
D O I
暂无
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The marine ecosystem is able to provide enormous biomolecule diversity that could be used for treatment of various diseases. In this highly competitive environment, organisms need chemical barriers to reduce or avoid microorganism contamination. Among the molecules that protect these animals the antimicrobial peptides (AMPs) are included. In the present study, crude extracts of coral coral specimens Carijoa riisei, Muriceopsis sulphurea, Neospongodes atlantica, Palythoa caribeorum, Phyllogorgia dilatata and Plexaurella grandiflora were challenged against multiple Gram-positive and -negative bacteria showing different activities. P. dilatata crude extract showed the antibacterial activity, and was ammonium-sulfate (0-40%) fractionated, being able to control the growth of K. pneumoniae, S. flexineri and S. aureus. Rich-fraction was further purified by using Amicon (R) Ultra Centrifugal 10 kDa associated with reversed-phase HPLC chromatography (C18), producing the peptide named Pd-AMP1. Pd-AMP1 was able to inhibit S. aureus development. Mass spectrometry analyses showed a monoisotopic mass of 5372.66 Da and N-terminal sequence showed no significant match with databank. In this view, the prospecting of protein biomolecules and biotechnological potential from marine animals is still little explored and may serve as an alternative to common antibiotics.
引用
收藏
页码:1153 / 1158
页数:6
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