Inducing the formation of a colloidal albumin carrier of curcumin

The administration and delivery of pharmaceuticals faces a variety of well-known obstacles that result in limited biocompatibility and bioavailability. Efforts to improve these properties have often employed serum albumin, primarily due to its inherent biocompatibility and its ability to enhance the...

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Main Authors: Konstantina Matskou, Berke Kisaoglan, Barbara Mavroidi, Maria Pelecanou, Maria Zoumpanioti, Ilias Matis, Aristotelis Xenakis
Format: Article
Language:English
Published: Elsevier 2022-07-01
Series:JCIS Open
Subjects:
Online Access:http://www.sciencedirect.com/science/article/pii/S2666934X22000095
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author Konstantina Matskou
Berke Kisaoglan
Barbara Mavroidi
Maria Pelecanou
Maria Zoumpanioti
Ilias Matis
Aristotelis Xenakis
author_facet Konstantina Matskou
Berke Kisaoglan
Barbara Mavroidi
Maria Pelecanou
Maria Zoumpanioti
Ilias Matis
Aristotelis Xenakis
author_sort Konstantina Matskou
collection DOAJ
description The administration and delivery of pharmaceuticals faces a variety of well-known obstacles that result in limited biocompatibility and bioavailability. Efforts to improve these properties have often employed serum albumin, primarily due to its inherent biocompatibility and its ability to enhance the circulation times of pharmaceuticals. In this work, we have adapted a nanoparticle-formulation protocol, to produce a protein carrier of curcumin with bovine serum albumin. This was achieved by using a near-equimolar protein:curcumin ratio instead of the abundance of curcumin that would be normally used in a nanoparticle formulation. Photometric and quantitative analysis of this carrier showed an increased curcumin content in the produced aqueous solutions following the homogenization of bovine serum albumin (water) and curcumin (dichloromethane) phases. Albumin fluorescence studies indicated curcumin association near a tryptophan residue, without excluding the possibility of additional sites. Circular dichroism provided strong evidence of this association through the induced circular dichroism effect and showed that the secondary structure of bovine serum albumin was effectively maintained. Overall, this work presented a new means of facilitating the association of increased levels of curcumin with bovine serum albumin, which could potentially be used to generate additional non-covalent albumin carriers for pharmaceutical compounds.
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spelling doaj.art-c091520aec2648f4b2ca1f60f91925312022-12-22T02:28:46ZengElsevierJCIS Open2666-934X2022-07-016100051Inducing the formation of a colloidal albumin carrier of curcuminKonstantina Matskou0Berke Kisaoglan1Barbara Mavroidi2Maria Pelecanou3Maria Zoumpanioti4Ilias Matis5Aristotelis Xenakis6Institute of Chemical Biology, National Hellenic Research Foundation, Athens, 11635, Greece; Department of Biology, National Kapodistrian University of Athens, Athens, 15701, GreeceInstitute of Chemical Biology, National Hellenic Research Foundation, Athens, 11635, GreeceInstitute of Biosciences and Applications, National Center for Scientific Research “Demokritos”, Athens, 15341, GreeceInstitute of Biosciences and Applications, National Center for Scientific Research “Demokritos”, Athens, 15341, GreeceInstitute of Chemical Biology, National Hellenic Research Foundation, Athens, 11635, GreeceInstitute of Chemical Biology, National Hellenic Research Foundation, Athens, 11635, Greece; Corresponding author.Institute of Chemical Biology, National Hellenic Research Foundation, Athens, 11635, Greece; Corresponding author. National Hellenic Research Foundation, Institute of Chemical Biology, 48, Vassileos Constantinou Av., 11635 Athens, Greece.The administration and delivery of pharmaceuticals faces a variety of well-known obstacles that result in limited biocompatibility and bioavailability. Efforts to improve these properties have often employed serum albumin, primarily due to its inherent biocompatibility and its ability to enhance the circulation times of pharmaceuticals. In this work, we have adapted a nanoparticle-formulation protocol, to produce a protein carrier of curcumin with bovine serum albumin. This was achieved by using a near-equimolar protein:curcumin ratio instead of the abundance of curcumin that would be normally used in a nanoparticle formulation. Photometric and quantitative analysis of this carrier showed an increased curcumin content in the produced aqueous solutions following the homogenization of bovine serum albumin (water) and curcumin (dichloromethane) phases. Albumin fluorescence studies indicated curcumin association near a tryptophan residue, without excluding the possibility of additional sites. Circular dichroism provided strong evidence of this association through the induced circular dichroism effect and showed that the secondary structure of bovine serum albumin was effectively maintained. Overall, this work presented a new means of facilitating the association of increased levels of curcumin with bovine serum albumin, which could potentially be used to generate additional non-covalent albumin carriers for pharmaceutical compounds.http://www.sciencedirect.com/science/article/pii/S2666934X22000095Bovine serum albuminHomogenizationNon-covalent associationEquimolar protein-binder
spellingShingle Konstantina Matskou
Berke Kisaoglan
Barbara Mavroidi
Maria Pelecanou
Maria Zoumpanioti
Ilias Matis
Aristotelis Xenakis
Inducing the formation of a colloidal albumin carrier of curcumin
JCIS Open
Bovine serum albumin
Homogenization
Non-covalent association
Equimolar protein-binder
title Inducing the formation of a colloidal albumin carrier of curcumin
title_full Inducing the formation of a colloidal albumin carrier of curcumin
title_fullStr Inducing the formation of a colloidal albumin carrier of curcumin
title_full_unstemmed Inducing the formation of a colloidal albumin carrier of curcumin
title_short Inducing the formation of a colloidal albumin carrier of curcumin
title_sort inducing the formation of a colloidal albumin carrier of curcumin
topic Bovine serum albumin
Homogenization
Non-covalent association
Equimolar protein-binder
url http://www.sciencedirect.com/science/article/pii/S2666934X22000095
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