Binding of HSA to macromolecular pHPMA based nanoparticles for drug delivery: an investigation using fluorescence methods

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61389013%3A_____%2F18%3A00491297" target="_blank" >RIV/61389013:_____/18:00491297 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1021/acs.langmuir.8b01015" target="_blank" >http://dx.doi.org/10.1021/acs.langmuir.8b01015</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1021/acs.langmuir.8b01015" target="_blank" >10.1021/acs.langmuir.8b01015</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Binding of HSA to macromolecular pHPMA based nanoparticles for drug delivery: an investigation using fluorescence methods

Popis výsledku v původním jazyce

Amphiphilic poly(N-(2-hydroxypropyl)methacrylamide) copolymers (pHPMA) bearing cholesterol side groups in phosphate buffer saline self-assemble into nanoparticles (NPs) which can be used as tumor-targeted drug carriers. It was previously shown by us that human serum albumin (HSA) interacts weakly with the NPs. However, the mechanism of this binding could not be resolved due to overlapping of signals from the complex system. Here, we use fluorescence labeling to distinguish the components and to characterize the binding: On the one hand, a fluorescent dye was attached to pHPMA, so that the diffusion behavior of the NPs could be studied in the presence of HSA using fluorescence lifetime correlation spectroscopy. On the other hand, quenching of the intrinsic fluorescence of HSA revealed the origin of the binding, which is mainly the complexation between HSA and cholesterol side groups. Furthermore, a binding constant was obtained.

Název v anglickém jazyce

Binding of HSA to macromolecular pHPMA based nanoparticles for drug delivery: an investigation using fluorescence methods

Popis výsledku anglicky

Amphiphilic poly(N-(2-hydroxypropyl)methacrylamide) copolymers (pHPMA) bearing cholesterol side groups in phosphate buffer saline self-assemble into nanoparticles (NPs) which can be used as tumor-targeted drug carriers. It was previously shown by us that human serum albumin (HSA) interacts weakly with the NPs. However, the mechanism of this binding could not be resolved due to overlapping of signals from the complex system. Here, we use fluorescence labeling to distinguish the components and to characterize the binding: On the one hand, a fluorescent dye was attached to pHPMA, so that the diffusion behavior of the NPs could be studied in the presence of HSA using fluorescence lifetime correlation spectroscopy. On the other hand, quenching of the intrinsic fluorescence of HSA revealed the origin of the binding, which is mainly the complexation between HSA and cholesterol side groups. Furthermore, a binding constant was obtained.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10404 - Polymer science

Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Rok uplatnění

2018

Kód důvěrnosti údajů

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

Název periodika

Langmuir

ISSN

0743-7463

e-ISSN

—

Svazek periodika

34

Číslo periodika v rámci svazku

27

Stát vydavatele periodika

US - Spojené státy americké

Počet stran výsledku

9

Strana od-do

7998-8006

Kód UT WoS článku

000438653800006

EID výsledku v databázi Scopus

2-s2.0-85049753519