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Adepantins, computationally designed, glycine-rich peptide antibiotics, with low toxicity and very high G- selectivity (CROSBI ID 598769)

Prilog sa skupa u zborniku | sažetak izlaganja sa skupa | međunarodna recenzija

Ilić, Nada ; Novković, Mario ; Guida, Filomena ; Xhindoli, Daniela ; Benincasa, Monica ; Tossi, Alessandro ; Juretić, Davor Adepantins, computationally designed, glycine-rich peptide antibiotics, with low toxicity and very high G- selectivity // New Antimicrobials Workshop in Trieste, 25-26.5.2012 / Tossi, Alessandro (ur.). Trst: Edizioni Università di Trieste, 2012. str. 37-38

Podaci o odgovornosti

Ilić, Nada ; Novković, Mario ; Guida, Filomena ; Xhindoli, Daniela ; Benincasa, Monica ; Tossi, Alessandro ; Juretić, Davor

engleski

Adepantins, computationally designed, glycine-rich peptide antibiotics, with low toxicity and very high G- selectivity

Adepantins (ADPs) are glycine-rich antimicrobial peptides (AMPs), constructed using the “Designer” algorithm, which is based on known characteristics of anuran AMPs [1]. Parameters used to predict the primary structure of ADPs include various physicochemical properties, such as lengthwise asymmetry and predicted therapeutic index (TI). ADP1 was previously tested and has shown high antimicrobial activity (MIC) against E. coli (2-4 microM) and low cytotoxic activity (HC50) against human red blood cells (480 microM). To confirm the high selectivity of peptides from this group, additional tests were performed for monomeric, dimeric and fluorescently labelled versions of ADP2 and ADP3, using different bacterial strains, host cells and model membrane systems. They are selective for Gram-negative bacterial cells (MIC = 0.5 - 4 microM) both with respect to human erythrocytes (HC50 > 400 microM for monomers), as with ADP1, and with respect to Gram-positive bacteria (MIC > 128 microM). Dimers have high haemolicity and exceptional antimicrobial activity. All adepantins structure as alpha helices when in contact with PG/dPG liposomes, while maintaining a random coil structure in the presence of PC/SM/Ch membranes. At sub-toxic concentrations, dimers exhibit much higher permeabilization of both bacterial membranes in various E. coli strains than monomers. The “Designer” algorithm thus identified novel AMPs less than 50% homologous to any other natural or synthetic AMP, highly selective for Gram-negative bacteria and with a high TI (up to 400). [1] D. Juretić, D. Vukičević, N. Ilić, N. Antcheva, A. Tossi, Computational design of highly selective antimicrobial peptides, J Chem Inf Model. 49, 2873-2882 (2009)

adepantins; peptide antibiotics; therapeutic index

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Podaci o prilogu

37-38.

2012.

objavljeno

Podaci o matičnoj publikaciji

New Antimicrobials Workshop in Trieste, 25-26.5.2012

Tossi, Alessandro

Trst: Edizioni Università di Trieste

978-88-8303-379-7

Podaci o skupu

New Antimicrobials Project 2-nd Workshop. New Compounds & New Strategies for Antimicrobials

poster

25.05.2012-26.05.2012

Trst, Italija

Povezanost rada

Fizika, Kemija, Biologija