About: Effect of hydrocarbon stapling on the properties of alpha-helical antimicrobial peptides isolated from the venom of hymenoptera     Goto   Sponge   NotDistinct   Permalink

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  • Introducing all-hydrocarbon staples into short alpha-helical amphipathic antimicrobial peptides increases their hydrophobicity, hydrophobic moment, rigidity and generally alpha-helicity in water. Stapling generally makes the peptides more resistant to proteolytic degradation, particularly those that are doubly stapled. The introduction of olefinic amino acid residues and conformational restriction by stapling make the peptides significantly more hemolytic, and lead to a decrease of their antimicrobial potency against pathogenic bacteria. Unfortunately, the stapling of those peptides is not rendering compounds that would have better pharmacological qualities than the native unmodified potent peptides.
  • Introducing all-hydrocarbon staples into short alpha-helical amphipathic antimicrobial peptides increases their hydrophobicity, hydrophobic moment, rigidity and generally alpha-helicity in water. Stapling generally makes the peptides more resistant to proteolytic degradation, particularly those that are doubly stapled. The introduction of olefinic amino acid residues and conformational restriction by stapling make the peptides significantly more hemolytic, and lead to a decrease of their antimicrobial potency against pathogenic bacteria. Unfortunately, the stapling of those peptides is not rendering compounds that would have better pharmacological qualities than the native unmodified potent peptides. (en)
Title
  • Effect of hydrocarbon stapling on the properties of alpha-helical antimicrobial peptides isolated from the venom of hymenoptera
  • Effect of hydrocarbon stapling on the properties of alpha-helical antimicrobial peptides isolated from the venom of hymenoptera (en)
skos:prefLabel
  • Effect of hydrocarbon stapling on the properties of alpha-helical antimicrobial peptides isolated from the venom of hymenoptera
  • Effect of hydrocarbon stapling on the properties of alpha-helical antimicrobial peptides isolated from the venom of hymenoptera (en)
skos:notation
  • RIV/61388963:_____/12:00384565!RIV13-AV0-61388963
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • P(GA203/08/0536), Z(AV0Z40550506)
http://linked.open...iv/cisloPeriodika
  • 5
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
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http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 133085
http://linked.open...ai/riv/idVysledku
  • RIV/61388963:_____/12:00384565
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • antimicrobial peptides; stapled peptides; amphipathic helix; CD spectroscopy (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • AT - Rakouská republika
http://linked.open...ontrolniKodProRIV
  • [517735E41A45]
http://linked.open...i/riv/nazevZdroje
  • Amino Acids
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http://linked.open...vavai/riv/projekt
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 43
http://linked.open...iv/tvurceVysledku
  • Bednárová, Lucie
  • Buděšínský, Miloš
  • Monincová, Lenka
  • Slaninová, Jiřina
  • Čeřovský, Václav
  • Chapuis, Hubert Jean
http://linked.open...ain/vavai/riv/wos
  • 000309863400022
http://linked.open...n/vavai/riv/zamer
issn
  • 0939-4451
number of pages
http://bibframe.org/vocab/doi
  • 10.1007/s00726-012-1283-1
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