Polymer-modified gene delivery vectors retargeted with recombinant proteins
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61389013%3A_____%2F12%3A00381465" target="_blank" >RIV/61389013:_____/12:00381465 - isvavai.cz</a>
Výsledek na webu
<a href="http://www.appleacademicpress.com/title.php?id=9781926895178" target="_blank" >http://www.appleacademicpress.com/title.php?id=9781926895178</a>
DOI - Digital Object Identifier
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Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Polymer-modified gene delivery vectors retargeted with recombinant proteins
Popis výsledku v původním jazyce
We have prepared and characterized a multivalent reactive N-(2-hydroxypropyl)methacrylamide copolymer (PHPMA) bearing bungarotoxin-binding peptide (BTXbp). The polymer was used for covalent surface modification of adenoviral vectors containing luciferasereporter gene (Ad). The peptide BTXbp is known to have extremely high binding affinity to bungarotoxin (BTX) ?a protein strongly binding to acetylcholine receptors. A recombinant protein consisting of antiPSMA antibody scFv fragment and BTX binding site(BTX-scFv) was used for retargeting of the polymer-modified Ad to prostate-specific membrane antigen (PSMA) receptors. While the polymer-modified Ad exhibited approximately 100-fold lower infectivity than the naked virus (in terms of luciferase expression), the addition of BTX-scFv to the polymer-coated Ad led to about 10-fold restoration of luciferase expression in PSMA-positive LNCaP cells. No such increase of transduction activity was observed in PSMA-negative PC3 cells. We have show
Název v anglickém jazyce
Polymer-modified gene delivery vectors retargeted with recombinant proteins
Popis výsledku anglicky
We have prepared and characterized a multivalent reactive N-(2-hydroxypropyl)methacrylamide copolymer (PHPMA) bearing bungarotoxin-binding peptide (BTXbp). The polymer was used for covalent surface modification of adenoviral vectors containing luciferasereporter gene (Ad). The peptide BTXbp is known to have extremely high binding affinity to bungarotoxin (BTX) ?a protein strongly binding to acetylcholine receptors. A recombinant protein consisting of antiPSMA antibody scFv fragment and BTX binding site(BTX-scFv) was used for retargeting of the polymer-modified Ad to prostate-specific membrane antigen (PSMA) receptors. While the polymer-modified Ad exhibited approximately 100-fold lower infectivity than the naked virus (in terms of luciferase expression), the addition of BTX-scFv to the polymer-coated Ad led to about 10-fold restoration of luciferase expression in PSMA-positive LNCaP cells. No such increase of transduction activity was observed in PSMA-negative PC3 cells. We have show
Klasifikace
Druh
C - Kapitola v odborné knize
CEP obor
CD - Makromolekulární chemie
OECD FORD obor
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Návaznosti výsledku
Projekt
Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.
Návaznosti
Z - Vyzkumny zamer (s odkazem do CEZ)
Ostatní
Rok uplatnění
2012
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název knihy nebo sborníku
Nanomedicine and Drug Delivery
ISBN
978-1-926895-17-8
Počet stran výsledku
6
Strana od-do
33-38
Počet stran knihy
320
Název nakladatele
Apple Academic Press
Místo vydání
Oakville
Kód UT WoS kapitoly
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