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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| Acceso en línea: | http://hdl.handle.net/20.500.12110/paper_15733149_v20_n3_p365_FlorezCastillo |
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todo:paper_15733149_v20_n3_p365_FlorezCastillo2023-10-03T16:27:34Z Enhancing antibacterial activity against Escherichia coli K-12 of peptide Ib-AMP4 with synthetic analogues Flórez-Castillo, J.M. Perullini, M. Jobbágy, M. De Jesús Cano Calle, H. 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 Escherichia coli K12 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 methionine, which resulted in a decrease in the number of synthesis byproducts, and consequently diminished the subsequent purification steps. The obtained peptides were purified by RP-HPLC and their molecular mass was determined by MALDI-TOF mass spectrometry. The peptide analogues (IC 50 between 1 and 50 μM) presented a higher antibacterial activity against Escherichia coli K-12 than the native peptide (IC50 > 100 μM). The hemolytic activity of the peptide with the highest antibacterial efficacy presented no degradation of erythrocytes for a concentration of 1 μM that corresponds to its IC50 value. The results show that the synthesized peptides are good candidates for the treatment of diseases caused by E. coli. © 2014 Springer Science+Business Media. Fil:Perullini, M. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_15733149_v20_n3_p365_FlorezCastillo |
| institution |
Universidad de Buenos Aires |
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I-28 |
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R-134 |
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Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA) |
| topic |
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 Escherichia coli K12 |
| spellingShingle |
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 Escherichia coli K12 Flórez-Castillo, J.M. Perullini, M. Jobbágy, M. De Jesús Cano Calle, H. Enhancing antibacterial activity against Escherichia coli K-12 of peptide Ib-AMP4 with synthetic analogues |
| topic_facet |
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 Escherichia coli K12 |
| description |
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 methionine, which resulted in a decrease in the number of synthesis byproducts, and consequently diminished the subsequent purification steps. The obtained peptides were purified by RP-HPLC and their molecular mass was determined by MALDI-TOF mass spectrometry. The peptide analogues (IC 50 between 1 and 50 μM) presented a higher antibacterial activity against Escherichia coli K-12 than the native peptide (IC50 > 100 μM). The hemolytic activity of the peptide with the highest antibacterial efficacy presented no degradation of erythrocytes for a concentration of 1 μM that corresponds to its IC50 value. The results show that the synthesized peptides are good candidates for the treatment of diseases caused by E. coli. © 2014 Springer Science+Business Media. |
| format |
JOUR |
| author |
Flórez-Castillo, J.M. Perullini, M. Jobbágy, M. De Jesús Cano Calle, H. |
| author_facet |
Flórez-Castillo, J.M. Perullini, M. Jobbágy, M. De Jesús Cano Calle, H. |
| author_sort |
Flórez-Castillo, J.M. |
| title |
Enhancing antibacterial activity against Escherichia coli K-12 of peptide Ib-AMP4 with synthetic analogues |
| title_short |
Enhancing antibacterial activity against Escherichia coli K-12 of peptide Ib-AMP4 with synthetic analogues |
| title_full |
Enhancing antibacterial activity against Escherichia coli K-12 of peptide Ib-AMP4 with synthetic analogues |
| title_fullStr |
Enhancing antibacterial activity against Escherichia coli K-12 of peptide Ib-AMP4 with synthetic analogues |
| title_full_unstemmed |
Enhancing antibacterial activity against Escherichia coli K-12 of peptide Ib-AMP4 with synthetic analogues |
| title_sort |
enhancing antibacterial activity against escherichia coli k-12 of peptide ib-amp4 with synthetic analogues |
| url |
http://hdl.handle.net/20.500.12110/paper_15733149_v20_n3_p365_FlorezCastillo |
| work_keys_str_mv |
AT florezcastillojm enhancingantibacterialactivityagainstescherichiacolik12ofpeptideibamp4withsyntheticanalogues AT perullinim enhancingantibacterialactivityagainstescherichiacolik12ofpeptideibamp4withsyntheticanalogues AT jobbagym enhancingantibacterialactivityagainstescherichiacolik12ofpeptideibamp4withsyntheticanalogues AT dejesuscanocalleh enhancingantibacterialactivityagainstescherichiacolik12ofpeptideibamp4withsyntheticanalogues |
| _version_ |
1782024366312128512 |