Enhancing antibacterial activity against Escherichia coli K-12 of peptide Ib-AMP4 with synthetic analogues

A family of Ib-AMP4 peptide analogues was obtained by solid phase synthesis, modifying the net charge and hydrophobicity of C-terminal domain by replacing certain amino acidic residues by arginine and tryptophan. Additionally, disulfide bonds were eliminated by replacing the cysteine residues by met...

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Detalles Bibliográficos
Autores principales: Flórez-Castillo, J.M., Perullini, M., Jobbágy, M., De Jesús Cano Calle, H.
Formato: JOUR
Materias:
Antibacterial peptides
Escherichia coli
Ib-AMP
Modified peptides
arginine
cysteine
disulfide
Ib AMP4 peptide
Ib AMP4 peptide derivative
Ib M1 peptide
Ib M2 peptide
Ib M3 peptide
Ib M4 peptide
Ib M5 peptide
Ib M6 peptide
methionine
peptide derivative
polypeptide antibiotic agent
synthetic peptide
tryptophan
unclassified drug
amino acid substitution
antibacterial activity
article
carboxy terminal sequence
controlled study
disulfide bond
drug determination
drug efficacy
drug purification
drug synthesis
Escherichia coli K 12
hemolysis
human
human cell
hydrophobicity
IC 50
matrix assisted laser desorption ionization time of flight mass spectrometry
minimum inhibitory concentration
molecular weight
nonhuman
protein determination
protein domain
protein purification
protein synthesis
reversed phase high performance liquid chromatography
Escherichia coli K12
Acceso en línea:http://hdl.handle.net/20.500.12110/paper_15733149_v20_n3_p365_FlorezCastillo
Aporte de:
Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) de Universidad de Buenos Aires

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