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Your search keyword '"Aguilar, Marie-Isabel"' showing total 290 results
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20. Professor Edouard Nice.

Author

Wade, John D. and Aguilar, Marie-Isabel

Subjects
*MACROPHAGE colony-stimulating factor, *GROWTH factors, *DYSPLASIA, *HISTORY of chemistry, *ANTIMICROBIAL peptides, *MOLECULAR biology, *HIPPO signaling pathway
Published
2023
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21. Differential membrane binding of α/β-peptide foldamers: implications for cellular delivery and mitochondrial targeting.

Author

Lee, Tzong-Hsien, Checco, James W., Malcolm, Tess, Eller, Chelcie H., Raines, Ronald T., Gellman, Samuel H., Lee, Erinna F., Fairlie, W. Douglas, and Aguilar, Marie-Isabel

Abstract

The intrinsic pathway of apoptosis is regulated by the Bcl-2 family of proteins. Inhibition of the anti-apoptotic members represents a strategy to induce apoptotic cell death in cancer cells. We have measured the membrane binding properties of a series of peptides, including modified α/β-peptides, designed to exhibit enhanced membrane permeability to allow cell entry and improved access for engagement of Bcl-2 family members. The peptide cargo is based on the pro-apoptotic protein Bim, which interacts with all anti-apoptotic proteins to initiate apoptosis. The α/β-peptides contained cyclic β-amino acid residues designed to increase their stability and membrane permeability. Dual polarisation interferometry was used to study the binding of each peptide to two different model membrane systems designed to mimic either the plasma membrane or the outer mitochondrial membrane. The impact of each peptide on the model membrane structure was also investigated, and the results demonstrated that the modified peptides had increased affinity for the mitochondrial membrane and significantly altered the structure of the bilayer. The results also showed that the presence of an RRR motif significantly enhanced the ability of the peptides to bind to and insert into the mitochondrial membrane mimic, and provide insights into the role of selective membrane targeting of peptides. The membrane binding of two peptides designed to exhibit enhanced membrane permeability to allow cell entry and engagement of Bcl-2 family members shows that an RRR motif significantly enhances peptide binding and insertion into a mitochondrial membrane mimic and provides insights into selective membrane targeting of peptides. [ABSTRACT FROM AUTHOR]

Published
2023
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41. The Novel AT2 Receptor Agonist β-Pro7-AngIII Exerts Cardiac and Renal Anti-Fibrotic and Anti-Inflammatory Effects in High Salt-Fed Mice.

Author

Wang, Yan, Yodgee, Jonathan, Del Borgo, Mark, Spizzo, Iresha, Nguyen, Levi, Aguilar, Marie-Isabel, Denton, Kate M., Samuel, Chrishan S., and Widdop, Robert E.

Subjects
RENAL fibrosis, HEART fibrosis, PEPTIDES, CARDIOVASCULAR diseases, MICE
Abstract

A high salt (HS) diet is associated with an increased risk for cardiovascular diseases (CVDs) and fibrosis is a key contributor to the organ dysfunction involved in CVDs. The activation of the renin angiotensin type 2 receptor (AT2R) has been considered as organ protective in many CVDs. However, there are limited AT2R-selective agonists available. Our first reported β-substituted angiotensin III peptide, β-Pro7-AngIII, showed high selectivity for the AT2R. In the current study, we examine the potential anti-fibrotic and anti-inflammatory effects of this novel AT2R-selective peptide on HS-induced organ damage. FVB/N mice fed with a 5% HS diet for 8 weeks developed cardiac and renal fibrosis and inflammation, which were associated with increased TGF-β1 levels in heart, kidney and plasma. Four weeks' treatment (from weeks 5–8) with β-Pro7-AngIII inhibited the HS-induced cardiac and renal fibrosis and inflammation. These protective effects were accompanied by reduced local and systemic TGF-β1 as well as reduced cardiac myofibroblast differentiation. Importantly, the anti-fibrotic and anti-inflammatory effects caused by β-Pro7-AngIII were attenuated by the AT2R antagonist PD123319. These results demonstrate, for the first time, the cardio- and reno-protective roles of the AT2R-selective β-Pro7-AngIII, highlighting it as an important therapeutic that can target the AT2R to treat end-organ damage. [ABSTRACT FROM AUTHOR]

Published
2022
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