Influence of core and maltose surface modification of PEIs on their interaction with plasma proteins-Human serum albumin and lysozyme

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F44555601%3A13440%2F17%3A43892836" target="_blank" >RIV/44555601:13440/17:43892836 - isvavai.cz</a>

Výsledek na webu

<a href="http://www.sciencedirect.com/science/article/pii/S0927776516308797" target="_blank" >http://www.sciencedirect.com/science/article/pii/S0927776516308797</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.colsurfb.2016.12.042" target="_blank" >10.1016/j.colsurfb.2016.12.042</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Influence of core and maltose surface modification of PEIs on their interaction with plasma proteins-Human serum albumin and lysozyme

Popis výsledku v původním jazyce

Regardless of the route of administration, some or all of a therapeutic agent will appear in the blood stream, where it can act on blood cells and other components of the plasma. Recently we have shown that poly(ethylene imines) (PEls) which interact with plasma proteins are taken up into erythrocyte membranes. These observations led us to investigate the interactions between maltose functionalized hyperbranched PEls (PEI-Mal) and plasma proteins. Two model proteins were chosen human serum albumin (HSA) (albumins constitute similar to 60% of all plasma proteins), and lysozyme. HSA is a negatively charged 66 kDa protein at neutral pH, whereas lysozyme is a positively charged 14 kDa protein. Fluorescence quenching and changes in the conformation of the amino acid tryptophan, diameter and zeta potential of proteins were investigated to evaluate the interaction of PEI-Mal with proteins. PEI-Mal interacts with both types of proteins. The strength of dendritic glycopolymer interactions was generally weak, especially with lysozyme. Greater changes were found with HSA, mainly triggered by hydrogen bonds and the electrostatic interaction properties of dendritic glycopolymers. Moreover, the structure and the size of PEI-Mal macromolecules affected these interactions; larger macromolecules with more sugar groups (95% maltose units) interacted more strongly with proteins than smaller ones with lower sugar modification (33% maltose units). Due to (i) the proven overall low toxicity of sugar-modified PEls and, (ii) their ability to interact preferentially through hydrogen bonds with proteins&quot; of human plasma or possibly with other interesting protein targets, PEI-Mal is a good candidate for creating therapeutic nanoparticles in the fast developing field of nanomedicine. (C) 2017 Elsevier B.V. All rights reserved.

Název v anglickém jazyce

Influence of core and maltose surface modification of PEIs on their interaction with plasma proteins-Human serum albumin and lysozyme

Popis výsledku anglicky

Regardless of the route of administration, some or all of a therapeutic agent will appear in the blood stream, where it can act on blood cells and other components of the plasma. Recently we have shown that poly(ethylene imines) (PEls) which interact with plasma proteins are taken up into erythrocyte membranes. These observations led us to investigate the interactions between maltose functionalized hyperbranched PEls (PEI-Mal) and plasma proteins. Two model proteins were chosen human serum albumin (HSA) (albumins constitute similar to 60% of all plasma proteins), and lysozyme. HSA is a negatively charged 66 kDa protein at neutral pH, whereas lysozyme is a positively charged 14 kDa protein. Fluorescence quenching and changes in the conformation of the amino acid tryptophan, diameter and zeta potential of proteins were investigated to evaluate the interaction of PEI-Mal with proteins. PEI-Mal interacts with both types of proteins. The strength of dendritic glycopolymer interactions was generally weak, especially with lysozyme. Greater changes were found with HSA, mainly triggered by hydrogen bonds and the electrostatic interaction properties of dendritic glycopolymers. Moreover, the structure and the size of PEI-Mal macromolecules affected these interactions; larger macromolecules with more sugar groups (95% maltose units) interacted more strongly with proteins than smaller ones with lower sugar modification (33% maltose units). Due to (i) the proven overall low toxicity of sugar-modified PEls and, (ii) their ability to interact preferentially through hydrogen bonds with proteins&quot; of human plasma or possibly with other interesting protein targets, PEI-Mal is a good candidate for creating therapeutic nanoparticles in the fast developing field of nanomedicine. (C) 2017 Elsevier B.V. All rights reserved.

Druh

J_imp - Článek v periodiku v databázi Web of Science

CEP obor

—

OECD FORD obor

10608 - Biochemistry and molecular biology

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

2017

Kód důvěrnosti údajů

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

Název periodika

Colloids and Surfaces B-Biointerfaces

ISSN

0927-7765

e-ISSN

—

Svazek periodika

2017

Číslo periodika v rámci svazku

152

Stát vydavatele periodika

NL - Nizozemsko

Počet stran výsledku

11

Strana od-do

18-28

Kód UT WoS článku

000398014100003

EID výsledku v databázi Scopus

—