About: Coiled Coil Peptides and Polymer-Peptide Conjugates: Synthesis, Self-Assembly, Characterization and Potential in Drug Delivery Systems     Goto   Sponge   NotDistinct   Permalink

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Description
  • Coiled coils are a common structural motif in many natural proteins that can also be utilized in the design and preparation of drug delivery systems for the noncovalent connection of two macromolecules. In this work, two different pairs of peptides forming coiled coil hetero-oligomers were designed, synthesized, and characterized. While the peptide sequences (VAALEKE)(4) and (VAALKEK)(4) predominantly form coiled coil heterodimers with randomly orientated peptide chains, (IAALESE)(2)-IAALESKIAALESE and IAALK-SKIAALKSE-(IAALKSK)(2) tend to form higher hetero-oligomers with an antiparallel orientation of their peptide chains. The associative behavior of these peptides was studied in aqueous solutions using circular dichroism spectroscopy, size-exclusion chromatography, isothermal titration calorimetry and sedimentation analyses. The orientation of the peptide chains in the coiled coil heterodimers was assessed using fluorescence spectroscopy with fluorescence resonance energy transfer labels attached to the ends of the peptides. The formation of the heterodimer can be used as a general method for the selective noncovalent conjugation of a specific targeting moiety with various drug carrier systems; this process involves simple self-assembly in a physiological solution before drug administration. The preparation of targeted macromolecular therapeutics consisting of a synthetic polymer drug carrier and a recombinant protein targeting ligand is discussed.
  • Coiled coils are a common structural motif in many natural proteins that can also be utilized in the design and preparation of drug delivery systems for the noncovalent connection of two macromolecules. In this work, two different pairs of peptides forming coiled coil hetero-oligomers were designed, synthesized, and characterized. While the peptide sequences (VAALEKE)(4) and (VAALKEK)(4) predominantly form coiled coil heterodimers with randomly orientated peptide chains, (IAALESE)(2)-IAALESKIAALESE and IAALK-SKIAALKSE-(IAALKSK)(2) tend to form higher hetero-oligomers with an antiparallel orientation of their peptide chains. The associative behavior of these peptides was studied in aqueous solutions using circular dichroism spectroscopy, size-exclusion chromatography, isothermal titration calorimetry and sedimentation analyses. The orientation of the peptide chains in the coiled coil heterodimers was assessed using fluorescence spectroscopy with fluorescence resonance energy transfer labels attached to the ends of the peptides. The formation of the heterodimer can be used as a general method for the selective noncovalent conjugation of a specific targeting moiety with various drug carrier systems; this process involves simple self-assembly in a physiological solution before drug administration. The preparation of targeted macromolecular therapeutics consisting of a synthetic polymer drug carrier and a recombinant protein targeting ligand is discussed. (en)
Title
  • Coiled Coil Peptides and Polymer-Peptide Conjugates: Synthesis, Self-Assembly, Characterization and Potential in Drug Delivery Systems
  • Coiled Coil Peptides and Polymer-Peptide Conjugates: Synthesis, Self-Assembly, Characterization and Potential in Drug Delivery Systems (en)
skos:prefLabel
  • Coiled Coil Peptides and Polymer-Peptide Conjugates: Synthesis, Self-Assembly, Characterization and Potential in Drug Delivery Systems
  • Coiled Coil Peptides and Polymer-Peptide Conjugates: Synthesis, Self-Assembly, Characterization and Potential in Drug Delivery Systems (en)
skos:notation
  • RIV/00216208:11310/14:10288605!RIV15-MSM-11310___
http://linked.open...avai/riv/aktivita
http://linked.open...avai/riv/aktivity
  • I, P(GCP207/12/J030)
http://linked.open...iv/cisloPeriodika
  • 7
http://linked.open...vai/riv/dodaniDat
http://linked.open...aciTvurceVysledku
http://linked.open.../riv/druhVysledku
http://linked.open...iv/duvernostUdaju
http://linked.open...titaPredkladatele
http://linked.open...dnocenehoVysledku
  • 7708
http://linked.open...ai/riv/idVysledku
  • RIV/00216208:11310/14:10288605
http://linked.open...riv/jazykVysledku
http://linked.open.../riv/klicovaSlova
  • copolymers; attachment; association; therapeutics; stability; specificity; protein; sedimentation-velocity; analytical ultracentrifugation; isothermal titration calorimetry (en)
http://linked.open.../riv/klicoveSlovo
http://linked.open...odStatuVydavatele
  • US - Spojené státy americké
http://linked.open...ontrolniKodProRIV
  • [C2ACB744A0C1]
http://linked.open...i/riv/nazevZdroje
  • Biomacromolecules
http://linked.open...in/vavai/riv/obor
http://linked.open...ichTvurcuVysledku
http://linked.open...cetTvurcuVysledku
http://linked.open...vavai/riv/projekt
http://linked.open...UplatneniVysledku
http://linked.open...v/svazekPeriodika
  • 15
http://linked.open...iv/tvurceVysledku
  • Bednárová, Lucie
  • Laga, Richard
  • Pechar, Michal
  • Pola, Robert
  • Ulbrich, Karel
  • Vaněk, Ondřej
  • Braunová, Alena
  • Bogomolova, Anna
  • Filippov, Sergey K.
http://linked.open...ain/vavai/riv/wos
  • 000339090500027
issn
  • 1525-7797
number of pages
http://bibframe.org/vocab/doi
  • 10.1021/bm500436p
http://localhost/t...ganizacniJednotka
  • 11310
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