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Article ; Online: Localized apelin-17 analogue-bicelle interactions as a facilitator of membrane-catalyzed receptor recognition and binding.

Phạm, Trần Thanh Tâm / Murza, Alexandre / Marsault, Éric / Frampton, John P / Rainey, Jan K

Biochimica et biophysica acta. Biomembranes

2024 Volume 1866, Issue 3, Page(s) 184289

Abstract: The apelinergic system encompasses two peptide ligand families, apelin and apela, along with the apelin receptor (AR or APJ), a class A G-protein-coupled receptor. This system has diverse physiological effects, including modulating heart contraction, ... ...

Abstract	The apelinergic system encompasses two peptide ligand families, apelin and apela, along with the apelin receptor (AR or APJ), a class A G-protein-coupled receptor. This system has diverse physiological effects, including modulating heart contraction, vasodilation/constriction, glucose regulation, and vascular development, with involvement in a variety of pathological conditions. Apelin peptides have been previously shown to interact with and become structured upon binding to anionic micelles, consistent with a membrane-catalyzed mechanism of ligand-receptor binding. To overcome the challenges of observing nuclear magnetic resonance (NMR) spectroscopy signals of a dilute peptide in biological environments,
MeSH term(s)	Humans ; Apelin/metabolism ; Ligands ; HEK293 Cells ; Peptide Hormones/chemistry ; Catalysis
Chemical Substances	Apelin ; Ligands ; Peptide Hormones
Language	English
Publishing date	2024-01-24
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	60-7
ISSN	1879-2642 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2618 ; 1879-2650 ; 0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
ISSN (online)	1879-2642 ; 1879-2596 ; 1879-260X ; 1872-8006 ; 1879-2618 ; 1879-2650
ISSN	0006-3002 ; 0005-2728 ; 0005-2736 ; 0304-4165 ; 0167-4838 ; 1388-1981 ; 0167-4889 ; 0167-4781 ; 0304-419X ; 1570-9639 ; 0925-4439 ; 1874-9399
DOI	10.1016/j.bbamem.2024.184289
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Article ; Online: Comparative Analysis of Cyclization Techniques in Stapled Peptides: Structural Insights into Protein-Protein Interactions in a SARS-CoV-2 Spike RBD/hACE2 Model System.

Ferková, Sára / Froehlich, Ulrike / Nepveu-Traversy, Marie-Édith / Murza, Alexandre / Azad, Taha / Grandbois, Michel / Sarret, Philippe / Lavigne, Pierre / Boudreault, Pierre-Luc

International journal of molecular sciences

2023 Volume 25, Issue 1

Abstract: Medicinal chemistry is constantly searching for new approaches to develop more effective and targeted therapeutic molecules. The design of peptidomimetics is a promising emerging strategy that is aimed at developing peptides that mimic or modulate the ... ...

Abstract	Medicinal chemistry is constantly searching for new approaches to develop more effective and targeted therapeutic molecules. The design of peptidomimetics is a promising emerging strategy that is aimed at developing peptides that mimic or modulate the biological activity of proteins. Among these, stapled peptides stand out for their unique ability to stabilize highly frequent helical motifs, but they have failed to be systematically reported. Here, we exploit chemically diverse helix-inducing
MeSH term(s)	Humans ; COVID-19 ; Cyclization ; Lactams ; Peptides/pharmacology ; SARS-CoV-2 ; Triazoles
Chemical Substances	Lactams ; Peptides ; Triazoles
Language	English
Publishing date	2023-12-21
Publishing country	Switzerland
Document type	Comparative Study ; Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms25010166
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Article ; Online: From garden to lab: C-3 chemical modifications of tomatidine unveil broad-spectrum ATP synthase inhibitors to combat bacterial resistance.

Delbrouck, Julien A / Murza, Alexandre / Diachenko, Iryna / Ben Jamaa, Abdelkhalek / Devi, Runjun / Larose, Audrey / Chamberland, Suzanne / Malouin, François / Boudreault, Pierre-Luc

European journal of medicinal chemistry

2023 Volume 262, Page(s) 115886

Abstract: Antibiotic resistance is escalating alarmingly worldwide. Bacterial resistance mechanisms are surfacing and proliferating across the globe, jeopardizing our capacity to manage prevalent infectious illnesses. Without drastic measures, we risk entering a ... ...

Abstract	Antibiotic resistance is escalating alarmingly worldwide. Bacterial resistance mechanisms are surfacing and proliferating across the globe, jeopardizing our capacity to manage prevalent infectious illnesses. Without drastic measures, we risk entering a post-antibiotic era, where even trivial infections and injuries can cause death again. In this context, we have developed a new class of antibiotics based on tomatidine (TO), a natural product derived from tomato plants, with a novel mode of action by targeting bacterial ATP synthases. The first generation of compounds proved highly specific for small-colony variants (SCVs) of Staphylococcus aureus. However, optimization of this scaffold through extensive structure-activity relationship studies has enabled us to broaden its effectiveness to include both Gram-positive and Gram-negative bacteria. Notably, the results showed that specific C3-modification of TO could improve ATP synthase inhibition and also bypass the outer membrane barrier of Gram-negative bacteria to gain substantial growth inhibition including against multi-resistant strains.
MeSH term(s)	Anti-Bacterial Agents/pharmacology ; Anti-Bacterial Agents/chemistry ; Gardens ; Gram-Negative Bacteria ; Gram-Positive Bacteria ; Adenosine Triphosphate
Chemical Substances	Anti-Bacterial Agents ; tomatidine (2B73S48786) ; Adenosine Triphosphate (8L70Q75FXE)
Language	English
Publishing date	2023-10-27
Publishing country	France
Document type	Journal Article
ZDB-ID	188597-2
ISSN	1768-3254 ; 0009-4374 ; 0223-5234
ISSN (online)	1768-3254
ISSN	0009-4374 ; 0223-5234
DOI	10.1016/j.ejmech.2023.115886
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Article ; Online: Signaling Modulation via Minimal C-Terminal Modifications of Apelin-13.

Théroux, Léa / Van Den Hauwe, Robin / Trân, Kien / Fournier, Justin / Desgagné, Michael / Meneboo, Nathan / Lavallée, Alexis / Fröhlich, Ulrike / Côté, Jérôme / Hollanders, Charlie / Longpré, Jean-Michel / Murza, Alexandre / Marsault, Eric / Sarret, Philippe / Boudreault, Pierre-Luc / Ballet, Steven

ACS pharmacology & translational science

2023 Volume 6, Issue 2, Page(s) 290–305

Abstract: Apelin is an endogenous peptide that is involved in many diseases such as cardiovascular diseases, obesity, and cancer, which has made it an attractive target for drug discovery. Herein, we explore the penultimate and final sequence positions of [ ... ...

Abstract	Apelin is an endogenous peptide that is involved in many diseases such as cardiovascular diseases, obesity, and cancer, which has made it an attractive target for drug discovery. Herein, we explore the penultimate and final sequence positions of [Pyr
Language	English
Publishing date	2023-01-26
Publishing country	United States
Document type	Journal Article
ISSN	2575-9108
ISSN (online)	2575-9108
DOI	10.1021/acsptsci.2c00219
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Article ; Online: Optimization of Ketobenzothiazole-Based Type II Transmembrane Serine Protease Inhibitors to Block H1N1 Influenza Virus Replication.

Colombo, Éloïc / Désilets, Antoine / Hassanzadeh, Malihe / Lemieux, Gabriel / Marois, Isabelle / Cliche, Dominic / Delbrouck, Julien A / Murza, Alexandre / Jean, François / Marsault, Eric / Richter, Martin V / Leduc, Richard / Boudreault, Pierre-Luc

ChemMedChem

2023 Volume 19, Issue 2, Page(s) e202300458

Abstract: Human influenza viruses cause acute respiratory symptoms that can lead to death. Due to the emergence of antiviral drug-resistant strains, there is an urgent requirement for novel antiviral agents and innovative therapeutic strategies. Using the ... ...

Abstract	Human influenza viruses cause acute respiratory symptoms that can lead to death. Due to the emergence of antiviral drug-resistant strains, there is an urgent requirement for novel antiviral agents and innovative therapeutic strategies. Using the peptidomimetic ketobenzothiazole protease inhibitor RQAR-Kbt (IN-1, aka N-0100) as a starting point, we report how substituting P2 and P4 positions with natural and unnatural amino acids can modulate the inhibition potency toward matriptase, a prototypical type II transmembrane serine protease (TTSP) that acts as a priming protease for influenza viruses. We also introduced modifications of the peptidomimetics N-terminal groups, leading to significant improvements (from μM to nM, 60 times more potent than IN-1) in their ability to inhibit the replication of influenza H1N1 virus in the Calu-3 cell line derived from human lungs. The selectivity towards other proteases has been evaluated and explained using molecular modeling with a crystal structure recently obtained by our group. By targeting host cell TTSPs as a therapeutic approach, it may be possible to overcome the high mutational rate of influenza viruses and consequently prevent potential drug resistance.
MeSH term(s)	Humans ; Influenza A Virus, H1N1 Subtype ; Serine Proteinase Inhibitors/pharmacology ; Influenza A virus/physiology ; Serine Proteases/metabolism ; Influenza, Human/drug therapy ; Protease Inhibitors/pharmacology ; Virus Replication
Chemical Substances	Serine Proteinase Inhibitors ; Serine Proteases (EC 3.4.-) ; Protease Inhibitors
Language	English
Publishing date	2023-10-31
Publishing country	Germany
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2218496-X
ISSN	1860-7187 ; 1860-7179
ISSN (online)	1860-7187
ISSN	1860-7179
DOI	10.1002/cmdc.202300458
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Article ; Online: Inhibitors of type II transmembrane serine proteases in the treatment of diseases of the respiratory tract - A review of patent literature.

Murza, Alexandre / Dion, Sébastien P / Boudreault, Pierre-Luc / Désilets, Antoine / Leduc, Richard / Marsault, Éric

Expert opinion on therapeutic patents

2020 Volume 30, Issue 11, Page(s) 807–824

Abstract: Introduction: Type II transmembrane serine proteases (TTSPs) of the human respiratory tract generate high interest owing to their ability, among other roles, to cleave surface proteins of respiratory viruses. This step is critical in the viral invasion ... ...

Abstract	Introduction: Type II transmembrane serine proteases (TTSPs) of the human respiratory tract generate high interest owing to their ability, among other roles, to cleave surface proteins of respiratory viruses. This step is critical in the viral invasion of coronaviruses, including SARS-CoV-2 responsible for COVID-19, but also influenza viruses and reoviruses. Accordingly, these cell surface enzymes constitute appealing therapeutic targets to develop host-based therapeutics against respiratory viral diseases. Additionally, their deregulated levels or activity has been described in non-viral diseases such as fibrosis, cancer, and osteoarthritis, making them potential targets in these indications. Areas covered: Areas covered: This review includes WIPO-listed patents reporting small molecules and peptide-based inhibitors of type II transmembrane serine proteases of the respiratory tract. Expert opinion: Expert opinion: Several TTSPs of the respiratory tract represent attractive pharmacological targets in the treatment of respiratory infectious diseases (notably COVID-19 and influenza), but also against idiopathic pulmonary fibrosis and lung cancer. The current emphasis is primarily on TMPRSS2, matriptase, and hepsin, yet other TTSPs await validation. Compounds listed herein are predominantly peptidomimetic inhibitors, some with covalent reversible mechanisms of action and high potencies. Their selectivity profile, however, are often only partially characterized. Preclinical data are promising and warrant further advancement in the above diseases.
MeSH term(s)	COVID-19 ; Coronavirus Infections/complications ; Coronavirus Infections/drug therapy ; Humans ; Pandemics ; Patents as Topic ; Pneumonia, Viral/complications ; Pneumonia, Viral/drug therapy ; Respiratory Tract Diseases/drug therapy ; Respiratory Tract Diseases/enzymology ; Respiratory Tract Diseases/etiology ; Serine Endopeptidases/metabolism ; Serine Proteinase Inhibitors/therapeutic use
Chemical Substances	Serine Proteinase Inhibitors ; Serine Endopeptidases (EC 3.4.21.-) ; TMPRSS2 protein, human (EC 3.4.21.-)
Keywords	covid19
Language	English
Publishing date	2020-10-12
Publishing country	England
Document type	Journal Article ; Review
ZDB-ID	1186201-4
ISSN	1744-7674 ; 0962-2594 ; 1354-3776
ISSN (online)	1744-7674
ISSN	0962-2594 ; 1354-3776
DOI	10.1080/13543776.2020.1817390
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Article ; Online: Simultaneous Ligand and Receptor Tracking through NMR Spectroscopy Enabled by Distinct

Simmons, Jeffrey R / Murza, Alexandre / Lumsden, Michael D / Kenward, Calem / Marsault, Éric / Rainey, Jan K

International journal of molecular sciences

2019 Volume 20, Issue 15

Abstract: To probe ligand-receptor binding at the atomic-level, a frequent approach involves multidimensional nuclear magnetic resonance (NMR) spectroscopy experiments relying ... ...

Abstract	To probe ligand-receptor binding at the atomic-level, a frequent approach involves multidimensional nuclear magnetic resonance (NMR) spectroscopy experiments relying on
MeSH term(s)	Amino Acid Sequence ; Apelin Receptors/chemistry ; Apelin Receptors/metabolism ; Fluorine-19 Magnetic Resonance Imaging/methods ; Humans ; Ligands ; Molecular Imaging ; Molecular Structure ; Protein Binding ; Receptors, G-Protein-Coupled/chemistry ; Receptors, G-Protein-Coupled/metabolism ; Structure-Activity Relationship
Chemical Substances	Apelin Receptors ; Ligands ; Receptors, G-Protein-Coupled
Language	English
Publishing date	2019-07-26
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2019364-6
ISSN	1422-0067 ; 1422-0067 ; 1661-6596
ISSN (online)	1422-0067
ISSN	1422-0067 ; 1661-6596
DOI	10.3390/ijms20153658
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Article ; Online: Comparative Analysis of Cyclization Techniques in Stapled Peptides

Sára Ferková / Ulrike Froehlich / Marie-Édith Nepveu-Traversy / Alexandre Murza / Taha Azad / Michel Grandbois / Philippe Sarret / Pierre Lavigne / Pierre-Luc Boudreault

International Journal of Molecular Sciences, Vol 25, Iss 1, p

Structural Insights into Protein–Protein Interactions in a SARS-CoV-2 Spike RBD/hACE2 Model System

2023 Volume 166

Abstract	Medicinal chemistry is constantly searching for new approaches to develop more effective and targeted therapeutic molecules. The design of peptidomimetics is a promising emerging strategy that is aimed at developing peptides that mimic or modulate the biological activity of proteins. Among these, stapled peptides stand out for their unique ability to stabilize highly frequent helical motifs, but they have failed to be systematically reported. Here, we exploit chemically diverse helix-inducing i , i + 4 constraints—lactam, hydrocarbon, triazole, double triazole and thioether—on two distinct short sequences derived from the N-terminal peptidase domain of hACE2 upon structural characterization and in silico alanine scan. Our overall objective was to provide a sequence-independent comparison of α-helix-inducing staples using circular dichroism (CD) and nuclear magnetic resonance (NMR) spectroscopy. We identified a 9-mer lactam stapled peptide derived from the hACE2 sequence (His34-Gln42) capable of reaching its maximal helicity of 55% with antiviral activity in bioreporter- and pseudovirus-based inhibition assays. To the best of our knowledge, this study is the first comprehensive investigation comparing several cyclization methods with the goal of generating stapled peptides and correlating their secondary structures with PPI inhibitions using a highly topical model system (i.e., the interaction of SARS-CoV-2 Spike RBD with hACE2).
Keywords	peptidomimetics ; protein–protein interaction (PPI) ; SARS-CoV-2 ; circular dichroism (CD) ; nuclear magnetic resonance (NMR) ; Biology (General) ; QH301-705.5 ; Chemistry ; QD1-999
Subject code	540
Language	English
Publishing date	2023-12-01T00:00:00Z
Publisher	MDPI AG
Document type	Article ; Online
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Article ; Online: Data set describing the

Besserer-Offroy, Élie / Tétreault, Pascal / Brouillette, Rebecca L / René, Adeline / Murza, Alexandre / Fanelli, Roberto / Kirby, Karyn / Parent, Alexandre / Dubuc, Isabelle / Beaudet, Nicolas / Côté, Jérôme / Longpré, Jean-Michel / Martinez, Jean / Cavelier, Florine / Sarret, Philippe

Data in brief

2020 Volume 31, Page(s) 105884

Abstract: Neurotensin (NT) is a tridecapeptide displaying interesting antinociceptive properties through its action on its receptors, NTS1 and NTS2. Neurotensin-like compounds have been shown to exert better antinociceptive properties than morphine at equimolar ... ...

Abstract	Neurotensin (NT) is a tridecapeptide displaying interesting antinociceptive properties through its action on its receptors, NTS1 and NTS2. Neurotensin-like compounds have been shown to exert better antinociceptive properties than morphine at equimolar doses. In this article, we characterized the molecular effects of a novel neurotensin (8-13) (NT(8-13)) analog containing an unnatural amino acid. This compound, named JMV2009, displays a Silaproline in position 10 in replacement of a proline in the native NT(8-13). We first examined the binding affinities of this novel NT(8-13) derivative at both NTS1 and NTS2 receptor sites by performing competitive displacement of iodinated NT on purified cell membranes. Then, we evaluated the ability of JMV2009 to activate NTS1-related G proteins as well as to promote the recruitment of β-arrestins 1 and 2 by using BRET-based cellular assays in live cells. We next assessed its ability to induce p42/p44 MAPK phosphorylation and NT receptors internalization using western blot and cell-surface ELISA, respectively. Finally, we determined the
Language	English
Publishing date	2020-06-20
Publishing country	Netherlands
Document type	Journal Article
ZDB-ID	2786545-9
ISSN	2352-3409 ; 2352-3409
ISSN (online)	2352-3409
ISSN	2352-3409
DOI	10.1016/j.dib.2020.105884
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Article ; Online: Size-Reduced Macrocyclic Analogues of [Pyr

Tran, Kien / Sainsily, Xavier / Côté, Jérôme / Coquerel, David / Couvineau, Pierre / Saibi, Sabrina / Haroune, Lounès / Besserer-Offroy, Élie / Flynn-Robitaille, Joël / Resua Rojas, Martin / Murza, Alexandre / Longpré, Jean-Michel / Auger-Messier, Mannix / Lesur, Olivier / Bouvier, Michel / Marsault, Éric / Boudreault, Pierre-Luc / Sarret, Philippe

Journal of medicinal chemistry

2022 Volume 65, Issue 1, Page(s) 531–551

Abstract: We previously reported a series of macrocyclic analogues of [ ... ...

Abstract	We previously reported a series of macrocyclic analogues of [Pyr
MeSH term(s)	Apelin/analogs & derivatives ; Apelin/pharmacokinetics ; Apelin/pharmacology ; Apelin Receptors/drug effects ; Arrestin/drug effects ; GTP-Binding Protein alpha Subunits, G12-G13/drug effects ; HEK293 Cells ; Half-Life ; Heart/drug effects ; Humans ; Injections, Subcutaneous ; Macrocyclic Compounds/chemical synthesis ; Macrocyclic Compounds/pharmacology ; Molecular Weight ; Signal Transduction/drug effects
Chemical Substances	Apelin ; Apelin Receptors ; Arrestin ; Macrocyclic Compounds ; GTP-Binding Protein alpha Subunits, G12-G13 (EC 3.6.5.1)
Language	English
Publishing date	2022-01-04
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	218133-2
ISSN	1520-4804 ; 0022-2623
ISSN (online)	1520-4804
ISSN	0022-2623
DOI	10.1021/acs.jmedchem.1c01708
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