Please use this identifier to cite or link to this item: https://repository.udca.edu.co/handle/11158/3502
Title: Shorter antibacterial peptide having high selectivity for e. Coli membranes and low potential for inducing resistance
Authors: Barreto Santamaría, Adriana
Rivera Monroy, Zuly Jenny
García Castañeda, Javier Eduardo
Curtidor, Hernando
Patarroyo, Manuel Elkin
Patarroyo, Manuel A.
Arevalo Pinzon, Gabriela
Issue Date: 2020
Citation: Barreto-Santamaría, A., Rivera, Z. J., García, J. E., Curtidor, H., Patarroyo, M. E., Patarroyo, M. A., & Arévalo-Pinzón, G. (2020). Shorter antibacterial peptide having high selectivity for e. coli membranes and low potential for inducing resistance. Microorganisms, 8(6), 1-21. doi:10.3390/microorganisms8060867
Series/Report no.: Microorganisms;Vol. 8, No. 6, Jun 2020, Article number 867, páginas 1-21
Abstract: Antimicrobial peptides (AMPs) have been recognised as a significant therapeutic option for mitigating resistant microbial infections. It has been found recently that Plasmodium falciparum-derived, 20 residue long, peptide 35409 had antibacterial and haemolytic activity, making it an AMP having reduced selectivity, and suggesting that it should be studied more extensively for obtaining new AMPs having activity solely targeting the bacterial membrane. Peptide 35409 was thus used as template for producing short synthetic peptides (<20 residues long) and evaluating their biological activity and relevant physicochemical characteristics for therapeutic use. Four of the sixteen short peptides evaluated here had activity against E. coli without any associated haemolytic effects. The 35409-1 derivative (17 residues long) had the best therapeutic characteristics as it had high selectivity for bacterial cells, stability in the presence of human sera, activity against E. coli multiresistant clinical isolates and was shorter than the original sequence. It had a powerful membranolytic effect and low potential for inducing resistance in bacteria. This peptide’s characteristics highlighted its potential as an alternative for combating infection caused by E. coli multiresistant bacteria and/or for designing new AMPs.
URI: https://www.mdpi.com/2076-2607/8/6/867
Appears in Collections:CCB. Artículos indexados en Scopus

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