Inducing the formation of a colloidal albumin carrier of curcumin

Q3 Materials Science
Konstantina Matskou , Berke Kisaoglan , Barbara Mavroidi , Maria Pelecanou , Maria Zoumpanioti , Ilias Matis , Aristotelis Xenakis
{"title":"Inducing the formation of a colloidal albumin carrier of curcumin","authors":"Konstantina Matskou ,&nbsp;Berke Kisaoglan ,&nbsp;Barbara Mavroidi ,&nbsp;Maria Pelecanou ,&nbsp;Maria Zoumpanioti ,&nbsp;Ilias Matis ,&nbsp;Aristotelis Xenakis","doi":"10.1016/j.jciso.2022.100051","DOIUrl":null,"url":null,"abstract":"<div><p>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.</p></div>","PeriodicalId":73541,"journal":{"name":"JCIS open","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2022-07-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2666934X22000095/pdfft?md5=41f79d90df8468b08f9974c45f546ef8&pid=1-s2.0-S2666934X22000095-main.pdf","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"JCIS open","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S2666934X22000095","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"Materials Science","Score":null,"Total":0}
引用次数: 0

Abstract

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.

Abstract Image

姜黄素胶体白蛋白载体的诱导形成
药物的管理和递送面临着各种众所周知的障碍,导致有限的生物相容性和生物利用度。改善这些特性的努力通常采用血清白蛋白,主要是由于其固有的生物相容性和提高药物循环时间的能力。在这项工作中,我们采用了纳米颗粒配方方案,用牛血清白蛋白生产姜黄素的蛋白质载体。这是通过使用接近等摩尔的蛋白质:姜黄素比例来实现的,而不是通常在纳米颗粒配方中使用的姜黄素丰度。该载体的光度和定量分析表明,在牛血清白蛋白(水)和姜黄素(二氯甲烷)相均质后,所制备的水溶液中姜黄素含量增加。白蛋白荧光研究表明姜黄素在色氨酸残基附近有关联,不排除其他位点的可能性。圆二色性通过诱导的圆二色性效应提供了这种关联的有力证据,表明牛血清白蛋白的二级结构得到了有效的维持。总的来说,这项工作提供了一种促进姜黄素与牛血清白蛋白水平增加的新方法,这可能被用于产生药物化合物的额外的非共价白蛋白载体。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
求助全文
约1分钟内获得全文 求助全文
来源期刊
JCIS open
JCIS open Physical and Theoretical Chemistry, Colloid and Surface Chemistry, Surfaces, Coatings and Films
CiteScore
4.10
自引率
0.00%
发文量
0
审稿时长
36 days
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信