Inhibition of amyloid fibrillation, enzymatic degradation and cytotoxicity of insulin at carboxyl tailored gold-aryl nanoparticles surface
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F60461373%3A22340%2F20%3A43934127" target="_blank" >RIV/60461373:22340/20:43934127 - isvavai.cz</a>
Result on the web
<a href="https://doi.org/10.1016/j.colsurfa.2019.124279" target="_blank" >https://doi.org/10.1016/j.colsurfa.2019.124279</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.colsurfa.2019.124279" target="_blank" >10.1016/j.colsurfa.2019.124279</a>
Alternative languages
Result language
angličtina
Original language name
Inhibition of amyloid fibrillation, enzymatic degradation and cytotoxicity of insulin at carboxyl tailored gold-aryl nanoparticles surface
Original language description
Insulin fibrillation complicated its oral delivery in diabetes therapy. pH sensitive carboxylate-terminated gold-carbon nanoparticles, AuNPs-C6H4-4-COOH, inhibited amyloid fibrillation and disintegrated the preformed insulin fibrils under amyloidogenic conditions. Transmission electron microscopy and X-ray photoelectron spectroscopy results support the immobilization of insulin on the nanoparticles surface. In contrast to native insulin, gold insulin bioconjugate exhibited a significant inhibitory effect against the proteolytic enzymatic activity of pepsin and trypsin while passaging through the stomach and gastrointestinal tract. Fluorescence solution studies supported the insulin fibrils dissociation over the gold nanoparticles surface in the presence of thioflavin T dye. In addition, fluorescence quenching studies were carried out to estimate the binding constant and the number of binding sites in insulin available for the gold nanoparticles. The outstanding hemocompatibility of the insulin bioconjugate in the presence of diabetic and non-diabetic red blood cells supports its significance in insulin drug delivery. With the aid of molecular docking calculations, we were able to verify the mediation of hydrophobic and hydrogen bonding interactions of benzoic acid with the fibril-forming region of insulin, which prevents these residues from the unfolding necessary for fibrillation. The robust gold-carbon nanoparticles mediation can be extended to defibrillate other proteins with nanomedicine therapies in Alzheimer’s, Parkinson’s, Huntington’s and infectious prion diseases.
Czech name
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Czech description
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Classification
Type
J<sub>imp</sub> - Article in a specialist periodical, which is included in the Web of Science database
CEP classification
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OECD FORD branch
10406 - Analytical chemistry
Result continuities
Project
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Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2020
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Name of the periodical
COLLOIDS AND SURFACES A-PHYSICOCHEMICAL AND ENGINEERING ASPECTS
ISSN
0927-7757
e-ISSN
1873-4359
Volume of the periodical
586
Issue of the periodical within the volume
5 February 2020
Country of publishing house
NL - THE KINGDOM OF THE NETHERLANDS
Number of pages
11
Pages from-to
nestránkováno
UT code for WoS article
000504350600010
EID of the result in the Scopus database
2-s2.0-85076220295