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Host defense peptides as natural product scaffolds for a design of next generation antibiotic classes (CROSBI ID 620333)

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

Juretić, Davor Host defense peptides as natural product scaffolds for a design of next generation antibiotic classes // Proceedings of the First Adriatic Symposium on Biophysical Approaches in Biomedical Studies / Raguž, Marija ; Kalyanaraman, Balaraman ; Sarna, Tadeusz et al. (ur.). Split: Mediterranean Institute for Life Sciences (MedILS), 2014. str. 53-53

Podaci o odgovornosti

Juretić, Davor

engleski

Host defense peptides as natural product scaffolds for a design of next generation antibiotic classes

An alarming drop in discoveries of new antibiotic scaffolds has occurred during last forty years, precisely at the time of accelerated development and worldwide spread of bacterial resistance. Host defense peptides (HDP) have all of desired drug attributes: fast acting (often with broad spectrum activity), low spontaneous resistance rates, amenability to generations of chemical tailoring and no cross-resistance to existing antibiotics. Synthetic peptides derived from HDF have been shown to exhibit synergistic or additive effects when combined with classical antibiotics. We took care to improve what has been lacking for HDF of non-human origin: a rational means (algorithms) for decreasing their toxicity to human cells and increasing their selectivity against bacterial cells. During last several years this effort resulted in finding dozen peptide antibiotics with high therapeutic index, such as adepantins, ascaphin-8 and XT-7 double substitution analogues, hfp1 and its analogues, trichoplaxin and kiadin, all designed by using evolutionary information stored in frog, fish and placozoa antimicrobial peptides. With completely different primary structure, these peptides pose biophysical challenge to find specificity/selectivity determinants from their membrane-associated 3D structure. To facilitate additional discoveries, we provide free for use on-line web server for in silico design of potential peptide antibiotics: http://split4.pmfst.hr/mutator/.

bacterial resistance; host defense peptides; peptide antibiotics; therapeutic index; computational design; web server

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Podaci o prilogu

53-53.

2014.

objavljeno

Podaci o matičnoj publikaciji

Proceedings of the First Adriatic Symposium on Biophysical Approaches in Biomedical Studies

Raguž, Marija ; Kalyanaraman, Balaraman ; Sarna, Tadeusz ; Ilić, Nada ; Nejašmić, Danijel ; Thelaner, Jane

Split: Mediterranean Institute for Life Sciences (MedILS)

978-953-55188-2-2

Podaci o skupu

First Adriatic Symposium on Biophysical Approaches in Biomedical Studies

pozvano predavanje

24.08.2014-29.08.2014

Split, Hrvatska

Povezanost rada

Fizika, Kemija, Biologija