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-[Ru(phen)(3,4Apy)]与模型脂质膜的结合：对新型抗淀粉样蛋白药物开发工具的启示。

Binding of -[Ru(phen)(3,4Apy)] to Model Lipid Membranes: Implications for New Tools in the Development of Antiamyloid Drugs.

作者信息

da Cruz Garcia Maria Laura, Paixão Rafaela Ribeiro, Pazin Wallance M, Oliveira Osvaldo N, Cremer Paul S, Carlos Rose Maria

机构信息

Department of Chemistry, Federal University of São Carlos, CP 676, CEP, São Carlos, São Paulo 13565-905, Brazil.

Department of Physics and Metereology, São Paulo State University, CEP, Bauru, São Paulo 17033-360, Brazil.

出版信息

Langmuir. 2024 Dec 31;40(52):27345-27355. doi: 10.1021/acs.langmuir.4c03552. Epub 2024 Dec 16.

DOI:10.1021/acs.langmuir.4c03552
PMID:39682054
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11697347/
Abstract

This study explores the interactions of the -[Ru(phen)(Apy)] complex (RuApy, phen = 1,10-phenanthroline, Apy = 3,4-aminopyridine) with model lipid membranes to explain the role this complex plays in mitigating Aβ toxicity in PC12 neuronal cells. Fluorescence quenching, surface pressure isotherms in Langmuir monolayers, and infrared reflection-absorption analyses revealed that the positively charged RuApy interacts with the phosphate headgroups of monolayers, indirectly affecting ester carbonyl groups through hydrogen bonding with the amino group of the pyridine ligand of RuApy. These results offer a scenario for the protective effect of RuApy against Aβ toxicity in neuronal cells in which these interactions shield the electrostatic interactions of Aβ with lipid membranes, preserving membrane integrity and mitigating the deleterious influence of Aβ. This opens new avenues for antiamyloid strategies, focusing on compounds that prevent salt-bridge formation between bilayer membranes and amyloid proteins, aiding in the rational design of effective antiamyloid agents for therapeutic application.

摘要

本研究探讨了-[Ru(phen)(Apy)]配合物（RuApy，phen = 1,10-菲咯啉，Apy = 3,4-氨基吡啶）与模型脂质膜的相互作用，以解释该配合物在减轻PC12神经元细胞中Aβ毒性方面所起的作用。荧光猝灭、Langmuir单分子层中的表面压力等温线以及红外反射吸收分析表明，带正电荷的RuApy与单分子层的磷酸头部基团相互作用，通过与RuApy吡啶配体的氨基形成氢键间接影响酯羰基。这些结果为RuApy对神经元细胞中Aβ毒性的保护作用提供了一种设想，即这些相互作用屏蔽了Aβ与脂质膜的静电相互作用，保持了膜的完整性并减轻了Aβ的有害影响。这为抗淀粉样蛋白策略开辟了新途径，重点关注防止双层膜与淀粉样蛋白之间形成盐桥的化合物，有助于合理设计用于治疗应用的有效抗淀粉样蛋白药物。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b96/11697347/fc5812cc5e94/la4c03552_0008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b96/11697347/9daf05ae0a08/la4c03552_0009.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b96/11697347/eac6052991e4/la4c03552_0010.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b96/11697347/1d3bb6ad925f/la4c03552_0001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b96/11697347/5b2b0b2d3575/la4c03552_0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b96/11697347/ca7a6446a5cc/la4c03552_0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b96/11697347/967d86182d2f/la4c03552_0004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b96/11697347/82e9f219b5a1/la4c03552_0005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b96/11697347/4cb38576b593/la4c03552_0006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b96/11697347/85d15bc03f58/la4c03552_0007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b96/11697347/fc5812cc5e94/la4c03552_0008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b96/11697347/9daf05ae0a08/la4c03552_0009.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b96/11697347/eac6052991e4/la4c03552_0010.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b96/11697347/1d3bb6ad925f/la4c03552_0001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b96/11697347/5b2b0b2d3575/la4c03552_0002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b96/11697347/ca7a6446a5cc/la4c03552_0003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b96/11697347/967d86182d2f/la4c03552_0004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b96/11697347/82e9f219b5a1/la4c03552_0005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b96/11697347/4cb38576b593/la4c03552_0006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b96/11697347/85d15bc03f58/la4c03552_0007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/2b96/11697347/fc5812cc5e94/la4c03552_0008.jpg

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