Coiled Coil Peptides and Polymer-Peptide Conjugates: Synthesis, Self-Assembly, Characterization and Potential in Drug Delivery Systems

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216208%3A11310%2F14%3A10288605" target="_blank" >RIV/00216208:11310/14:10288605 - isvavai.cz</a>

Nalezeny alternativní kódy

RIV/61389013:_____/14:00429827 RIV/61388963:_____/14:00429827

Výsledek na webu

<a href="http://dx.doi.org/10.1021/bm500436p" target="_blank" >http://dx.doi.org/10.1021/bm500436p</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1021/bm500436p" target="_blank" >10.1021/bm500436p</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Coiled Coil Peptides and Polymer-Peptide Conjugates: Synthesis, Self-Assembly, Characterization and Potential in Drug Delivery Systems

Popis výsledku v původním jazyce

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 andIAALK-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-exclusionchromatography, 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 la

Název v anglickém jazyce

Coiled Coil Peptides and Polymer-Peptide Conjugates: Synthesis, Self-Assembly, Characterization and Potential in Drug Delivery Systems

Popis výsledku anglicky

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 andIAALK-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-exclusionchromatography, 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 la

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

CD - Makromolekulární chemie

OECD FORD obor

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Projekt

<a href="/cs/project/GCP207%2F12%2FJ030" target="_blank" >GCP207/12/J030: Vysoce účinná polymerní terapeutika na bázi nanonosičů reagujících na vnější stimuly</a><br>

Návaznosti

I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace

Rok uplatnění

2014

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Biomacromolecules

ISSN

1525-7797

e-ISSN

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Svazek periodika

15

Číslo periodika v rámci svazku

7

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

10

Strana od-do

2590-2599

Kód UT WoS článku

000339090500027

EID výsledku v databázi Scopus

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