研究一种与表面结合的亲和结合的稀土元素,该源自兰莫杜林EF-Hand Loop I的EF-Hand Loop I
Geeta Verma1, Jacob Hostert1, Alex A Summerville1
1Department of Chemical and Biomolecular Engineering, Case Western Reserve University, Cleveland, Ohio 44106, United States.
ACS applied materials & interfaces
|March 25, 2024
概括
模仿兰莫杜林的生物灵感对稀土元素 (REEs) 具有很高的选择性. 固定化保持强烈的REE结合亲和力,为从废物流中回收REE提供可持续的解决方案.
科学领域:
- 生物启发材料科学 生物启发材料科学
- 用于资源回收的生物技术.
- 稀土元素的分离 稀土元素的分离
背景情况:
- 生物启发策略提供从废物中可持续和选择性回收稀土元素 (REEs).
- 兰莫杜林蛋白具有很高的REE选择性,但更简单的仿真物对于实际应用是可取的.
- 对于先进的分离技术来说,对固体基板上的兰莫杜林衍生的固定至关重要,但仍未得到充分探索.
研究的目的:
- 设计和研究兰莫杜林衍生 (LanM1和编码LanM1) 的REE结合亲和力.
- 为了评估固定LanM1在固体表面的性能,以捕获REE.
- 为了证明表面结合的LanM1在REE与溶液分离中的实际实用性.
主要方法:
- 循环二元化 (CD),核磁共振 (NMR),分子动力学 (MD) 和异热定位热量计 (ITC) 用于基于溶液的结合特性.
- 石英晶体微平衡与消散 (QCM-D) 以评估在黄金表面上的固定性能.
- 使用Arsenazo III和UV-Vis光谱光度测试对金纳米粒子 (GNPs) 的REE捕获实验进行色度测量染料位移测定.
主要成果:
- 在溶液和固定状态下,LanM1表现出比混合的LanM1更强的REE结合亲和力.
- 固定的LanM1对REEs (Ce(III),Nd(III),Eu(III),Y(III) 保持了很高的亲和力,对竞争对手离子 (Ca(II),Cu(II)) 没有亲和力.
- 支持黄金纳米粒子的LanM1实现了目标REEs的和吸附能力约为3.5μmolREE/g.
结论:
- 在固体基板上固定时,兰莫杜林衍生 (LanM1) 有效地结合稀土元素.
- 表面的LanM1提供了可再生能源的选择性和高亲和度捕获,证明了废物流回收的潜力.
- 这项研究验证了生物灵感的使用,用于开发先进的REE分离技术.
相关概念视频
Ligand Binding Sites
12.8K
Proteins are dynamic macromolecules that carry out a wide variety of essential processes; however, the activities of most proteins depend on their interactions with other molecules or ions, known as ligands.
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
Protein-ligand interactions are quite specific; even though numerous potential ligands surround a cellular protein at any given time, only a particular ligand can bind to that protein. Moreover, a ligand binds only to a dedicated area on the surface of the protein, known as the...
12.8K
Conserved Binding Sites
4.2K
Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
4.2K
Ligand Binding and Linkage
4.8K
Allosteric proteins have more than one ligand binding site; the binding of a ligand to any of these sites influences the binding of ligands to the other sites. When a protein is allosteric, its binding sites are called coupled or linked. In the case of enzymes, the site that binds to the substrate is known as the active site and the other site is known as the regulatory site. When a ligand binds to the regulatory site, this leads to conformational changes in the protein that can influence...
4.8K
Tail-anchoring of Proteins in the ER Membrane
3.1K
Tail-anchored, or TA, proteins are estimated to make up to 3-5% of membrane proteins found in the eukaryotic cell. Such proteins have a single transmembrane domain located approximately 30 amino acid residues upstream from the C-terminal end. As a result, the signal recognition particle (SRP) cannot guide a TA protein to the ER membrane for cotranslational insertion. Hence, they are integrated into the ER membrane post-translationally using their C-terminal end as the anchor. TA proteins...
3.1K
Calmodulin-dependent Signaling
5.1K
Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
5.1K
Transducer Mechanism: Enzyme-Linked Receptors
2.5K
Enzyme-linked receptors are cell-surface receptors acting as an enzyme or associating with an enzyme intracellularly. They make excellent drug targets. Drugs can bind to the extracellular ligand-binding domain or directly affect their enzymatic domain and alter their activity.
Major types that are helpful drug targets include:
Major types that are helpful drug targets include:
2.5K


