Magnetic relaxometry of methemoglobin by widefield nitrogen-vacancy microscopy

IF 3.5 2区 物理与天体物理 Q2 PHYSICS, APPLIED
Suvechhya Lamichhane, Evelyn Carreto Guevara, Ilja Fescenko, Sy-Hwang Liou, Rebecca Y. Lai, Abdelghani Laraoui
{"title":"Magnetic relaxometry of methemoglobin by widefield nitrogen-vacancy microscopy","authors":"Suvechhya Lamichhane, Evelyn Carreto Guevara, Ilja Fescenko, Sy-Hwang Liou, Rebecca Y. Lai, Abdelghani Laraoui","doi":"10.1063/5.0217987","DOIUrl":null,"url":null,"abstract":"Hemoglobin (Hb) is a multifaceted protein, classified as a metalloprotein, chromoprotein, and globulin. It incorporates iron, which plays a crucial role in transporting oxygen within red blood cells. Hb functions by carrying oxygen from the respiratory organs to diverse tissues in the body, where it releases oxygen to fuel aerobic respiration, thus supporting the organism's metabolic processes. Hb can exist in several forms, primarily distinguished by the oxidation state of the iron in the heme group, including methemoglobin (MetHb). Measuring the concentration of MetHb is crucial because it cannot transport oxygen; hence, higher concentrations of MetHb in the blood causes methemoglobinemia. Here, we use optically detected magnetic relaxometry of paramagnetic iron spins in MetHb drop-cast onto a nanostructured diamond doped with shallow high-density nitrogen-vacancy (NV) spin qubits. We vary the concentration of MetHb in the range of 6 × 106–1.8 × 107 adsorbed Fe+3 spins per micrometer squared and observe an increase in the NV relaxation rate Γ1 (=1/T1, where T1 is the NV spin lattice relaxation time) up to 2 × 103 s−1. NV magnetic relaxometry of MetHb in phosphate-buffered saline solution shows a similar effect with an increase in Γ1 to 6.7 × 103 s−1 upon increasing the MetHb concentration to 100 μM. The increase in NV Γ1 is explained by the increased spin noise coming from the Fe+3 spins present in MetHb proteins. This study presents an additional usage of NV quantum sensors to detect paramagnetic centers of biomolecules at volumes below 100 picoliter.","PeriodicalId":8094,"journal":{"name":"Applied Physics Letters","volume":null,"pages":null},"PeriodicalIF":3.5000,"publicationDate":"2024-09-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Applied Physics Letters","FirstCategoryId":"101","ListUrlMain":"https://doi.org/10.1063/5.0217987","RegionNum":2,"RegionCategory":"物理与天体物理","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"PHYSICS, APPLIED","Score":null,"Total":0}
引用次数: 0

Abstract

Hemoglobin (Hb) is a multifaceted protein, classified as a metalloprotein, chromoprotein, and globulin. It incorporates iron, which plays a crucial role in transporting oxygen within red blood cells. Hb functions by carrying oxygen from the respiratory organs to diverse tissues in the body, where it releases oxygen to fuel aerobic respiration, thus supporting the organism's metabolic processes. Hb can exist in several forms, primarily distinguished by the oxidation state of the iron in the heme group, including methemoglobin (MetHb). Measuring the concentration of MetHb is crucial because it cannot transport oxygen; hence, higher concentrations of MetHb in the blood causes methemoglobinemia. Here, we use optically detected magnetic relaxometry of paramagnetic iron spins in MetHb drop-cast onto a nanostructured diamond doped with shallow high-density nitrogen-vacancy (NV) spin qubits. We vary the concentration of MetHb in the range of 6 × 106–1.8 × 107 adsorbed Fe+3 spins per micrometer squared and observe an increase in the NV relaxation rate Γ1 (=1/T1, where T1 is the NV spin lattice relaxation time) up to 2 × 103 s−1. NV magnetic relaxometry of MetHb in phosphate-buffered saline solution shows a similar effect with an increase in Γ1 to 6.7 × 103 s−1 upon increasing the MetHb concentration to 100 μM. The increase in NV Γ1 is explained by the increased spin noise coming from the Fe+3 spins present in MetHb proteins. This study presents an additional usage of NV quantum sensors to detect paramagnetic centers of biomolecules at volumes below 100 picoliter.
通过宽场氮空位显微镜测量高铁血红蛋白的磁弛度
血红蛋白(Hb)是一种多元蛋白质,分为金属蛋白、染色蛋白和球蛋白。它含有铁元素,铁元素在红血细胞内运输氧气的过程中起着至关重要的作用。Hb 的功能是将氧气从呼吸器官运送到身体的各种组织,并在这些组织中释放氧气,为有氧呼吸提供燃料,从而支持机体的新陈代谢过程。血红蛋白有多种存在形式,主要以血红素基团中铁的氧化状态来区分,其中包括高铁血红蛋白(MetHb)。测量高铁血红蛋白的浓度至关重要,因为高铁血红蛋白不能运输氧气;因此,血液中高铁血红蛋白浓度较高会导致高铁血红蛋白血症。在这里,我们使用光学检测法对滴铸在掺有浅层高密度氮空位(NV)自旋比特的纳米结构金刚石上的 MetHb 中的顺磁铁自旋进行磁弛豫测量。我们在每平方微米 6 × 106-1.8 × 107 的范围内改变 MetHb 的吸附 Fe+3 自旋浓度,观察到 NV 驰豫速率Γ1(=1/T1,其中 T1 是 NV 自旋晶格驰豫时间)增加到 2 × 103 s-1。磷酸盐缓冲盐溶液中 MetHb 的 NV 磁弛豫测定法也显示了类似的效果,当 MetHb 浓度增加到 100 μM 时,Γ1 增加到 6.7 × 103 s-1。NV Γ1 增加的原因是 MetHb 蛋白中存在的 Fe+3 自旋增加了自旋噪声。这项研究提供了另一种利用 NV 量子传感器检测体积低于 100 皮升的生物大分子顺磁中心的方法。
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
Applied Physics Letters
Applied Physics Letters 物理-物理:应用
CiteScore
6.40
自引率
10.00%
发文量
1821
审稿时长
1.6 months
期刊介绍: Applied Physics Letters (APL) features concise, up-to-date reports on significant new findings in applied physics. Emphasizing rapid dissemination of key data and new physical insights, APL offers prompt publication of new experimental and theoretical papers reporting applications of physics phenomena to all branches of science, engineering, and modern technology. In addition to regular articles, the journal also publishes invited Fast Track, Perspectives, and in-depth Editorials which report on cutting-edge areas in applied physics. APL Perspectives are forward-looking invited letters which highlight recent developments or discoveries. Emphasis is placed on very recent developments, potentially disruptive technologies, open questions and possible solutions. They also include a mini-roadmap detailing where the community should direct efforts in order for the phenomena to be viable for application and the challenges associated with meeting that performance threshold. Perspectives are characterized by personal viewpoints and opinions of recognized experts in the field. Fast Track articles are invited original research articles that report results that are particularly novel and important or provide a significant advancement in an emerging field. Because of the urgency and scientific importance of the work, the peer review process is accelerated. If, during the review process, it becomes apparent that the paper does not meet the Fast Track criterion, it is returned to a normal track.
×
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