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

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 f...

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Autores:
Tipo de recurso:
Fecha de publicación:
2009
Institución:
Universidad del Rosario
Repositorio:
Repositorio EdocUR - U. Rosario
Idioma:
eng
OAI Identifier:
oai:repository.urosario.edu.co:10336/22783
Acceso en línea:
https://doi.org/10.1016/j.peptides.2009.08.011
https://repository.urosario.edu.co/handle/10336/22783
Palabra clave:
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
Rights
License
Abierto (Texto Completo)