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A C-terminal cationic fragment derived from an arginine-rich peptide exhibits in vitro antibacterial and anti-plasmodial activities governed by its secondary structure properties

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Lesmes, Liliana Patricia
Bohorquez, Magda Yenith
Carreño, Luisa Fernanda
Patarroyo, Manuel Elkin
Lozano, José Manuel



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The differential in vitro antimicrobial activity of a 12-residue-long arginine-rich peptide derived from protamine was examined against bacterial and parasite microbes. A design of discrete peptide fragments based on the thermolysin-digestion map allowed us to propose three peptide fragments to be further assessed regarding their biological and secondary structural properties. Peptide structure allowed designing three arginine-rich fragments. All peptide fragments were assessed regarding their antimicrobial activity against Gram-positive and Gram-negative bacteria and a human malaria strain. Qualitative and quantitative assays carried out for determining all peptides' antibacterial activity at different concentration levels included radial diffusion and a time-controlled technique. Tests demonstrated that all assessed molecules inhibited invasion of Plasmodium falciparum parasites to human red blood cells. Cytolytic activity of the parent protamine peptide was completely abolished by strategically fragmenting its aminoacid sequence. Remarkably, the cationic C-fragment exhibited stronger biological activity than its parent peptide. Interestingly, the peptide fragment denoted as 2077 displays a typical ?-helix profile according to its CD spectrum. The results support proposing the protamine C-terminal fragment as a potential new antimicrobial peptide. © 2009 Elsevier Inc. All rights reserved.
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Ampicillin , Andropin , Antimicrobial peptide 2075 , Antimicrobial peptide 2076 , Antimicrobial peptide 2077 , Antimicrobial peptide mp 17 , Antimicrobial peptide mp 3 , Antimicrobial peptide mp 7 , Antimicrobial peptide mp 8 , Antimicrobial peptide mp x , Antimicrobial peptide pgla , Antimicrobial peptide tap , Apamin , Bombinin , Cecropin a , Cecropin b , Cecropin p1 , Criptidin , Dermaseptin , Kanamycin , Maganin 2 , Maganin i , Melittin , Polistes , Polistes ma , Polypeptide antibiotic agent , Protamine , Taquilepsin 1 , Thermolysin , Unclassified drug , Unindexed drug , Alpha helix , Amino acid sequence , Antibacterial activity , Antibiotic sensitivity , Antiprotozoal activity , Article , Carboxy terminal sequence , Concentration response , Controlled study , Cytolysis , Disk diffusion , Erythrocyte , Gram negative bacterium , Gram positive bacterium , Host parasite interaction , Human , Human cell , In vitro study , Nonhuman , Physical chemistry , Plasmodium falciparum , Priority journal , Protein secondary structure , Qualitative analysis , Quantitative analysis , Structure activity relation , Animals , Anti-bacterial agents , Antimalarials , Antimicrobial cationic peptides , Arginine , Erythrocytes , Humans , Microbial sensitivity tests , Plasmodium falciparum , Bacteria (microorganisms) , Negibacteria , Plasmodium falciparum , Posibacteria , ?-helix , Anti-plasmodial activity , Antimicrobial peptide , Arginine-rich peptide , Secondary structure
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