改性分子作为潜在的调节 Shelterin 蛋白功能; TRF1
Wioletta Brankiewicz1, Umesh Kalathiya2, Monikaben Padariya2
1Department of Pharmaceutical Technology and Biochemistry, Faculty of Chemistry, Gdansk University of Technology, Narutowicza St 11/12, 80-233, Gdansk, Poland.
Chemistry (Weinheim an der Bergstrasse, Germany)
|June 18, 2023
概括
针对shelterin蛋白中的TRF1-TIN2相互作用的新型类分子显示出对癌症治疗的前途. 阻止这种相互作用会诱导乳腺癌细胞中的细胞衰老,这表明一种新的化疗策略.
科学领域:
- 在瘤学瘤学.
- 分子生物学分子生物学
- 生物化学 生物化学
背景情况:
- 包括TRF1在内的庇护蛋白对于端粒维护至关重要.
- TRF1与TIN2的相互作用对于shelterin复合体的功能至关重要.
- 癌细胞经常表现出端粒不稳定性,使得庇护蛋白成为潜在的治疗点.
研究的目的:
- 为了研究新型皮多米米特分子作为TRF1-TIN2蛋白质-蛋白质相互作用的抑制剂.
- 探索调节TRF1-TIN2相互作用在癌症治疗中的治疗潜力.
主要方法:
- 在形设计的型模拟分子.
- 表面等离子体共振 (SPR) 实验以确认分子相互作用.
- 使用乳腺癌细胞系的体外研究.
主要成果:
- 在SPR实验中,一种改性,PEP1,被证明与TRF1相互作用,可能发生在TIN2结合部位.
- 抑制TRF1-TIN2相互作用并没有引起立即的细胞毒性.
- 阻止TRF1-TIN2相互作用导致乳腺癌细胞系中的细胞衰老.
结论:
- 研究的二胺化合物是开发TRF蛋白抑制剂的有效起点.
- 调节TRF1-TIN2相互作用可以诱导细胞衰老,这是一个潜在的抗癌机制.
- 针对shelterin复杂相互作用为新型癌症化疗提供了一个有希望的途径.
更多相关视频
08:48Development of a Backbone Cyclic Peptide Library as Potential Antiparasitic Therapeutics Using Microwave Irradiation
Published on: January 26, 2016
11.9K
11:09Constructing Thioether/Vinyl Sulfide-tethered Helical Peptides Via Photo-induced Thiol-ene/yne Hydrothiolation
Published on: August 1, 2018
10.8K
相关概念视频
Covalently Linked Protein Regulators
6.9K
Proteins can undergo many types of post-translational modifications, often in response to changes in their environment. These modifications play an important role in the function and stability of these proteins. Covalently linked molecules include functional groups, such as methyl, acetyl, and phosphate groups, and also small proteins, such as ubiquitin. There are around 200 different types of covalent regulators that have been identified.
These groups modify specific amino acids in a protein....
These groups modify specific amino acids in a protein....
6.9K
Translocation of Proteins into the Mitochondria
3.2K
Mitochondrial precursors are translocated to the internal subcompartments via independent mechanisms involving distinct protein machineries called translocases.
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
Sorting of outer membrane proteins:
Mitochondrial outer membrane proteins are of two types: the transmembrane, beta-barrel porins, and the membrane-anchored, alpha-helical proteins. Beta-barrel porin precursors are translocated by the TOM complex and inserted into the outer mitochondrial membrane by the SAM complex. In contrast,...
3.2K
Molecular Chaperones and Protein Folding
18.1K
The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
The...
The...
18.1K
