Effect of crosslinking chemistry of albumin/heparin multilayers on FGF-2 adsorption and endothelial cell behavior
Identifikátory výsledku
Kód výsledku v IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61389013%3A_____%2F17%3A00473967" target="_blank" >RIV/61389013:_____/17:00473967 - isvavai.cz</a>
Nalezeny alternativní kódy
RIV/68407700:21460/17:00311488
Výsledek na webu
<a href="http://dx.doi.org/10.1016/j.apsusc.2017.03.193" target="_blank" >http://dx.doi.org/10.1016/j.apsusc.2017.03.193</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.apsusc.2017.03.193" target="_blank" >10.1016/j.apsusc.2017.03.193</a>
Alternativní jazyky
Jazyk výsledku
angličtina
Název v původním jazyce
Effect of crosslinking chemistry of albumin/heparin multilayers on FGF-2 adsorption and endothelial cell behavior
Popis výsledku v původním jazyce
The biomaterials that efficiently deliver growth factors represent an important challenge in cell-based tissue engineering. Layer-by-layer (LbL) thin films are attractive for incorporating controlled amounts of growth factors and releasing them over time. Herein, we investigated the effect of a method of cross-linking of albumin/heparin layer-by-layer (LbL) assembly ((Alb/Hep)3) on the loading and release of basic fibroblast growth factor (FGF-2), and subsequent proliferation of human endothelial cells (HUVECs). The (Alb/Hep)3 assemblies were cross-linked using glutaraldehyde, reductive amination or carbodiimide chemistries, and then biofunctionalized with FGF-2. The (Alb/Hep)3 assemblies were characterized by the infrared multi-internal reflection spectroscopy, atomic force microscopy, ellipsometry, and surface plasmon resonance (SPR). The FGF-2 loading was quantified by the SPR in situ analysis. Our results showed that the (Alb/Hep)3 cross-linking affected the amount of the bound heparin (from 150 to 315 ng/cm2), amount of FGF-2 loaded (from 75 to 125 ng/cm2), FGF-2 release (from 15 to 53% over 8 days), and consequently the HUVEC cell proliferation (from 50 to 80 × 103 cells/cm2 at day 5). All FGF-2 loaded assemblies stimulated the cell growth more than a soluble FGF-2 added into the cell media. In particular, the highest HUVECs proliferation was detected on the carbodiimide-cross-linked assembly. Overall, these biocompatible cross-linked assemblies can fine-tune the loading and release of growth factor providing a platform for cell-contacting applications.
Název v anglickém jazyce
Effect of crosslinking chemistry of albumin/heparin multilayers on FGF-2 adsorption and endothelial cell behavior
Popis výsledku anglicky
The biomaterials that efficiently deliver growth factors represent an important challenge in cell-based tissue engineering. Layer-by-layer (LbL) thin films are attractive for incorporating controlled amounts of growth factors and releasing them over time. Herein, we investigated the effect of a method of cross-linking of albumin/heparin layer-by-layer (LbL) assembly ((Alb/Hep)3) on the loading and release of basic fibroblast growth factor (FGF-2), and subsequent proliferation of human endothelial cells (HUVECs). The (Alb/Hep)3 assemblies were cross-linked using glutaraldehyde, reductive amination or carbodiimide chemistries, and then biofunctionalized with FGF-2. The (Alb/Hep)3 assemblies were characterized by the infrared multi-internal reflection spectroscopy, atomic force microscopy, ellipsometry, and surface plasmon resonance (SPR). The FGF-2 loading was quantified by the SPR in situ analysis. Our results showed that the (Alb/Hep)3 cross-linking affected the amount of the bound heparin (from 150 to 315 ng/cm2), amount of FGF-2 loaded (from 75 to 125 ng/cm2), FGF-2 release (from 15 to 53% over 8 days), and consequently the HUVEC cell proliferation (from 50 to 80 × 103 cells/cm2 at day 5). All FGF-2 loaded assemblies stimulated the cell growth more than a soluble FGF-2 added into the cell media. In particular, the highest HUVECs proliferation was detected on the carbodiimide-cross-linked assembly. Overall, these biocompatible cross-linked assemblies can fine-tune the loading and release of growth factor providing a platform for cell-contacting applications.
Klasifikace
Druh
J<sub>imp</sub> - Článek v periodiku v databázi Web of Science
CEP obor
—
OECD FORD obor
10404 - Polymer science
Návaznosti výsledku
Projekt
Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.
Návaznosti
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Ostatní
Rok uplatnění
2017
Kód důvěrnosti údajů
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Údaje specifické pro druh výsledku
Název periodika
Applied Surface Science
ISSN
0169-4332
e-ISSN
—
Svazek periodika
411
Číslo periodika v rámci svazku
31 July
Stát vydavatele periodika
NL - Nizozemsko
Počet stran výsledku
11
Strana od-do
240-250
Kód UT WoS článku
000401391900030
EID výsledku v databázi Scopus
2-s2.0-85016429973