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

Result code in 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>

Result on the web

<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>

Result language

angličtina

Original language name

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

Original language description

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.

Czech name

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Czech description

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Type

J_imp - Article in a specialist periodical, which is included in the Web of Science database

CEP classification

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OECD FORD branch

10608 - Biochemistry and molecular biology

Project

Result was created during the realization of more than one project. More information in the Projects tab.

Continuities

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

Publication year

2017

Confidentiality

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

Name of the periodical

Colloids and Surfaces B-Biointerfaces

ISSN

0927-7765

e-ISSN

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Volume of the periodical

2017

Issue of the periodical within the volume

152

Country of publishing house

NL - THE KINGDOM OF THE NETHERLANDS

Number of pages

11

Pages from-to

18-28

UT code for WoS article

000398014100003

EID of the result in the Scopus database

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