A2 牛奶蛋白单层的有利界面特性

IF 2.3 4区 生物学 Q3 BIOCHEMISTRY & MOLECULAR BIOLOGY
Journal of Membrane Biology Pub Date : 2023-02-01 Epub Date: 2022-06-20 DOI:10.1007/s00232-022-00248-8
Balaji S Dhopte, V N Lad
{"title":"A2 牛奶蛋白单层的有利界面特性","authors":"Balaji S Dhopte, V N Lad","doi":"10.1007/s00232-022-00248-8","DOIUrl":null,"url":null,"abstract":"<p><p>Shielding of the specific body organ using the biocompatible material helps preventing direct exposure of that part to the foreign entities responsible for infections. Here we show the potential of the A2 milk protein recovered from the milk of cow from Indian origin for possible prevention of the direct exposure to other foreign molecules. We measured the surface pressure of the monolayers of different types of protein samples using Langmuir isotherm experiments. The surface pressure measurements for the monolayer of four types of protein macromolecules have been carried out using the Wilhelmy plate micro pressure sensor. We studied the self-organization of different protein macromolecules and their monolayer compression characteristics. The electrochemical behaviour is studied using electrochemical impedance spectroscopy. We found the highest surface pressure for the monolayer of A2 protein. Further, it is also found that A2 protein exhibited the highest surface activity amongst the other proteins. This property can be effectively used for making the envelope of the A2 protein surrounding the targeted entity.</p>","PeriodicalId":50129,"journal":{"name":"Journal of Membrane Biology","volume":"256 1","pages":"35-41"},"PeriodicalIF":2.3000,"publicationDate":"2023-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9208347/pdf/","citationCount":"0","resultStr":"{\"title\":\"Favourable Interfacial Characteristics of A2 Milk Protein Monolayer.\",\"authors\":\"Balaji S Dhopte, V N Lad\",\"doi\":\"10.1007/s00232-022-00248-8\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Shielding of the specific body organ using the biocompatible material helps preventing direct exposure of that part to the foreign entities responsible for infections. Here we show the potential of the A2 milk protein recovered from the milk of cow from Indian origin for possible prevention of the direct exposure to other foreign molecules. We measured the surface pressure of the monolayers of different types of protein samples using Langmuir isotherm experiments. The surface pressure measurements for the monolayer of four types of protein macromolecules have been carried out using the Wilhelmy plate micro pressure sensor. We studied the self-organization of different protein macromolecules and their monolayer compression characteristics. The electrochemical behaviour is studied using electrochemical impedance spectroscopy. We found the highest surface pressure for the monolayer of A2 protein. Further, it is also found that A2 protein exhibited the highest surface activity amongst the other proteins. This property can be effectively used for making the envelope of the A2 protein surrounding the targeted entity.</p>\",\"PeriodicalId\":50129,\"journal\":{\"name\":\"Journal of Membrane Biology\",\"volume\":\"256 1\",\"pages\":\"35-41\"},\"PeriodicalIF\":2.3000,\"publicationDate\":\"2023-02-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9208347/pdf/\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Membrane Biology\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.1007/s00232-022-00248-8\",\"RegionNum\":4,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2022/6/20 0:00:00\",\"PubModel\":\"Epub\",\"JCR\":\"Q3\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Membrane Biology","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1007/s00232-022-00248-8","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2022/6/20 0:00:00","PubModel":"Epub","JCR":"Q3","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0

摘要

使用生物相容性材料保护特定的身体器官有助于防止该器官直接暴露于导致感染的外来物质。在这里,我们展示了从印度牛乳中提取的 A2 牛奶蛋白在防止直接接触其他外来分子方面的潜力。我们利用朗缪尔等温线实验测量了不同类型蛋白质样品单层的表面压力。我们使用 Wilhelmy 平板微压力传感器测量了四种蛋白质大分子单层的表面压力。我们研究了不同蛋白质大分子的自组织及其单层压缩特性。我们使用电化学阻抗光谱对其电化学行为进行了研究。我们发现 A2 蛋白质单层的表面压力最高。此外,我们还发现 A2 蛋白在其他蛋白质中表现出最高的表面活性。这一特性可有效地用于制造环绕目标实体的 A2 蛋白包膜。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Favourable Interfacial Characteristics of A2 Milk Protein Monolayer.

Favourable Interfacial Characteristics of A2 Milk Protein Monolayer.

Favourable Interfacial Characteristics of A2 Milk Protein Monolayer.

Favourable Interfacial Characteristics of A2 Milk Protein Monolayer.

Shielding of the specific body organ using the biocompatible material helps preventing direct exposure of that part to the foreign entities responsible for infections. Here we show the potential of the A2 milk protein recovered from the milk of cow from Indian origin for possible prevention of the direct exposure to other foreign molecules. We measured the surface pressure of the monolayers of different types of protein samples using Langmuir isotherm experiments. The surface pressure measurements for the monolayer of four types of protein macromolecules have been carried out using the Wilhelmy plate micro pressure sensor. We studied the self-organization of different protein macromolecules and their monolayer compression characteristics. The electrochemical behaviour is studied using electrochemical impedance spectroscopy. We found the highest surface pressure for the monolayer of A2 protein. Further, it is also found that A2 protein exhibited the highest surface activity amongst the other proteins. This property can be effectively used for making the envelope of the A2 protein surrounding the targeted entity.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
Journal of Membrane Biology
Journal of Membrane Biology 生物-生化与分子生物学
CiteScore
4.80
自引率
4.20%
发文量
63
审稿时长
6-12 weeks
期刊介绍: The Journal of Membrane Biology is dedicated to publishing high-quality science related to membrane biology, biochemistry and biophysics. In particular, we welcome work that uses modern experimental or computational methods including but not limited to those with microscopy, diffraction, NMR, computer simulations, or biochemistry aimed at membrane associated or membrane embedded proteins or model membrane systems. These methods might be applied to study topics like membrane protein structure and function, membrane mediated or controlled signaling mechanisms, cell-cell communication via gap junctions, the behavior of proteins and lipids based on monolayer or bilayer systems, or genetic and regulatory mechanisms controlling membrane function. Research articles, short communications and reviews are all welcome. We also encourage authors to consider publishing ''negative'' results where experiments or simulations were well performed, but resulted in unusual or unexpected outcomes without obvious explanations. While we welcome connections to clinical studies, submissions that are primarily clinical in nature or that fail to make connections to the basic science issues of membrane structure, chemistry and function, are not appropriate for the journal. In a similar way, studies that are primarily descriptive and narratives of assays in a clinical or population study are best published in other journals. If you are not certain, it is entirely appropriate to write to us to inquire if your study is a good fit for the journal.
×
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