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Article ; Online: Small Molecules

Zhao, Yusheng / Rao, Praveen P N

ACS chemical neuroscience

2023 Volume 14, Issue 23, Page(s) 4185–4198

Abstract: This study reports the unusual ability of small ... ...

Abstract	This study reports the unusual ability of small molecules
MeSH term(s)	Humans ; Amyloid beta-Peptides/metabolism ; Peptide Fragments/metabolism ; Alzheimer Disease/metabolism ; Neurons/metabolism
Chemical Substances	amyloid beta-protein (1-42) ; Amyloid beta-Peptides ; Peptide Fragments
Language	English
Publishing date	2023-11-16
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1948-7193
ISSN (online)	1948-7193
DOI	10.1021/acschemneuro.3c00576
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Article ; Online: Differential Effects of Endocannabinoids on Amyloid-Beta Aggregation and Toxicity.

Khavandi, Marzie / Rao, Praveen P N / Beazely, Michael A

International journal of molecular sciences

2023 Volume 24, Issue 2

Abstract: The regulation and metabolism of the endocannabinoid system has received extensive attention for their potential neuroprotective effect in neurodegenerative diseases such as Alzheimer's disease (AD), which is characterized by amyloid β (Aβ) -induced cell ...

Abstract	The regulation and metabolism of the endocannabinoid system has received extensive attention for their potential neuroprotective effect in neurodegenerative diseases such as Alzheimer's disease (AD), which is characterized by amyloid β (Aβ) -induced cell toxicity, inflammation, and oxidative stress. Using in vitro techniques and two cell lines, the mouse hippocampus-derived HT22 cells and Chinese hamster ovary (CHO) cells expressing human cannabinoid receptor type 1 (CB1), we investigated the ability of endocannabinoids to inhibit Aβ aggregation and protect cells against Aβ toxicity. The present study provides evidence that endocannabinoids N-arachidonoyl ethanol amide (AEA), noladin and O-arachidonoyl ethanolamine (OAE) inhibit Aβ42 aggregation. They were able to provide protection against Aβ42 induced cytotoxicity via receptor-mediated and non-receptor-mediated mechanisms in CB1-CHO and HT22 cells, respectively. The aggregation kinetic experiments demonstrate the anti-Aβ aggregation activity of some endocannabinoids (AEA, noladin). These data demonstrate the potential role and application of endocannabinoids in AD pathology and treatment.
MeSH term(s)	Mice ; Animals ; Cricetinae ; Humans ; Endocannabinoids/pharmacology ; Endocannabinoids/metabolism ; Amyloid beta-Peptides/toxicity ; CHO Cells ; Cricetulus ; Alzheimer Disease/metabolism
Chemical Substances	Endocannabinoids ; Amyloid beta-Peptides
Language	English
Publishing date	2023-01-04
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/ijms24020911
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Article ; Online: Post-Translational Modifications in Tau and Their Roles in Alzheimer's Pathology.

Kalyaanamoorthy, Subha / Opare, Stanley Kojo / Xu, Xiaoxiao / Ganesan, Aravindhan / Rao, Praveen P N

Current Alzheimer research

2024

Abstract: Microtubule-Associated Protein Tau (also known as tau) has been shown to accumulate into paired helical filaments and neurofibrillary tangles, which are known hallmarks of Alzheimer's disease (AD) pathology. Decades of research have shown that tau ... ...

Abstract	Microtubule-Associated Protein Tau (also known as tau) has been shown to accumulate into paired helical filaments and neurofibrillary tangles, which are known hallmarks of Alzheimer's disease (AD) pathology. Decades of research have shown that tau protein undergoes extensive post-translational modifications (PTMs), which can alter the protein's structure, function, and dynamics and impact the various properties such as solubility, aggregation, localization, and homeostasis. There is a vast amount of information describing the impact and role of different PTMs in AD pathology and neuroprotection. However, the complex interplay between these PTMs remains elusive. Therefore, in this review, we aim to comprehend the key post-translational modifications occurring in tau and summarize potential connections to clarify their impact on the physiology and pathophysiology of tau. Further, we describe how different computational modeling methods have helped in understanding the impact of PTMs on the structure and functions of the tau protein. Finally, we highlight the tau PTM-related therapeutics strategies that are explored for the development of AD therapy.
Language	English
Publishing date	2024-04-15
Publishing country	United Arab Emirates
Document type	Journal Article
ZDB-ID	2205170-3
ISSN	1875-5828 ; 1567-2050
ISSN (online)	1875-5828
ISSN	1567-2050
DOI	10.2174/0115672050301407240408033046
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Article ; Online: Modeling the Inhibition Kinetics of Curcumin, Orange G, and Resveratrol with Amyloid-β Peptide.

Madhuranthakam, Chandra Mouli R / Shakeri, Arash / Rao, Praveen P N

ACS omega

2021 Volume 6, Issue 12, Page(s) 8680–8686

Abstract: The β-amyloid (Aβ) protein aggregation into toxic forms is one of the major factors in the Alzheimer's disease (AD) pathology. Screening compound libraries as inhibitors of Aβ-aggregation is a common strategy to discover novel molecules as potential ... ...

Abstract	The β-amyloid (Aβ) protein aggregation into toxic forms is one of the major factors in the Alzheimer's disease (AD) pathology. Screening compound libraries as inhibitors of Aβ-aggregation is a common strategy to discover novel molecules as potential therapeutics in AD. In this regard, thioflavin T (ThT)-based fluorescence spectroscopy is a widely used in vitro method to identify inhibitors of Aβ aggregation. However, conventional data processing of the ThT assay experimental results generally provides only qualitative output and lacks inhibitor-specific quantitative data, which can offer a number of advantages such as identification of critical inhibitor-specific parameters required to design superior inhibitors and reduce the need to conduct extensive in vitro kinetic studies. Therefore, we carried out mathematical modeling based on logistic equation and power law (PL) model to correlate the experimental results obtained from the ThT-based Aβ40 aggregation kinetics for small-molecule inhibitors curcumin, orange G, and resveratrol and quantitatively fit the data in a logistic equation. This approach provides important inhibitor-specific parameters such as lag time λ, inflection point τ, maximum slope
Language	English
Publishing date	2021-03-19
Publishing country	United States
Document type	Journal Article
ISSN	2470-1343
ISSN (online)	2470-1343
DOI	10.1021/acsomega.1c00610
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Article ; Online: Peptide-Modified Gemini Surfactants as Delivery System Building Blocks with Dual Functionalities for Glaucoma Treatment: Gene Carriers and Amyloid-Beta (Aβ) Self-Aggregation Inhibitors.

Narsineni, Lokesh / Rao, Praveen P N / Pham, Amy Trinh / Foldvari, Marianna

Molecular pharmaceutics

2022 Volume 19, Issue 8, Page(s) 2737–2753

Abstract: Retinal ganglion cell (RGC) neurodegeneration in glaucoma has potential links with amyloid-β (Aβ) deposition. Targeting the Aβ pathway was shown to reduce RGC apoptosis and protect RGCs from degeneration. We report exploratory studies on the amyloid ... ...

Abstract	Retinal ganglion cell (RGC) neurodegeneration in glaucoma has potential links with amyloid-β (Aβ) deposition. Targeting the Aβ pathway was shown to reduce RGC apoptosis and protect RGCs from degeneration. We report exploratory studies on the amyloid Aβ
MeSH term(s)	Amyloid beta-Peptides/metabolism ; Glaucoma/drug therapy ; Humans ; Hydrophobic and Hydrophilic Interactions ; Molecular Docking Simulation ; Peptide Fragments/metabolism ; Polymers ; Surface-Active Agents/chemistry
Chemical Substances	Amyloid beta-Peptides ; Peptide Fragments ; Polymers ; Surface-Active Agents
Language	English
Publishing date	2022-07-08
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2138405-8
ISSN	1543-8392 ; 1543-8384
ISSN (online)	1543-8392
ISSN	1543-8384
DOI	10.1021/acs.molpharmaceut.2c00088
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Article ; Online: Strategies in the design and development of (TAR) DNA-binding protein 43 (TDP-43) binding ligands.

Rao, Praveen P N / Shakeri, Arash / Zhao, Yusheng / Calon, Frederic

European journal of medicinal chemistry

2021 Volume 225, Page(s) 113753

Abstract: The human transactive responsive (TAR) DNA-binding protein 43 (TDP-43) is involved in a number of physiological processes in the body. Its primary function involves RNA regulation. The TDP-43 protein is also involved in many diseases such as amyotrophic ... ...

Abstract	The human transactive responsive (TAR) DNA-binding protein 43 (TDP-43) is involved in a number of physiological processes in the body. Its primary function involves RNA regulation. The TDP-43 protein is also involved in many diseases such as amyotrophic lateral sclerosis (ALS), frontotemporal dementia (FTD), Alzheimer's disease (AD), Parkinson's disease (PD) and even cancers. These TDP-43 mediated diseases are collectively called as TDP-43 proteinopathies. Intense research in the last decade has increased our understanding on TDP-43 structure and function in biology. The three-dimensional structures of TDP-43 domains such as N-terminal domain (NTD), RNA-recognition motif-1 (RRM1), RNA-recognition motif-2 (RRM2) and the C-terminal domain (CTD) or low-complexity domain (LCD) have been solved. These structures have yielded insights into novel binding sites and pockets at various TDP-43 domains, which can be targeted by designing a diverse library of ligands including small molecules, peptides and oligonucleotides as molecular tools to (i) study TDP-43 function, (ii) develop novel diagnostic agents and (iii) discover disease-modifying therapies to treat TDP-43 proteinopathies. This review provides a summary on recent progress in the development of TDP-43 binding ligands and uses the solved structures of various TDP-43 domains to investigate putative ligand binding regions that can be exploited to discover novel molecular probes to modulate TDP-43 structure and function.
MeSH term(s)	Animals ; DNA-Binding Proteins/antagonists & inhibitors ; DNA-Binding Proteins/chemistry ; DNA-Binding Proteins/metabolism ; Drug Development ; Humans ; Ligands ; Molecular Structure ; Oligonucleotides/chemical synthesis ; Oligonucleotides/chemistry ; Oligonucleotides/pharmacology ; Peptides/chemical synthesis ; Peptides/chemistry ; Peptides/pharmacology ; Small Molecule Libraries/chemical synthesis ; Small Molecule Libraries/chemistry ; Small Molecule Libraries/pharmacology
Chemical Substances	DNA-Binding Proteins ; Ligands ; Oligonucleotides ; Peptides ; Small Molecule Libraries
Language	English
Publishing date	2021-08-08
Publishing country	France
Document type	Journal Article ; Review
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.2021.113753
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Article ; Online: 2,4-Disubstituted quinazolines as amyloid-β aggregation inhibitors with dual cholinesterase inhibition and antioxidant properties: Development and structure-activity relationship (SAR) studies.

Mohamed, Tarek / Rao, Praveen P N

European journal of medicinal chemistry

2017 Volume 126, Page(s) 823–843

Abstract: A library of fifty-seven 2,4-disubstituted quinazoline derivatives were designed, synthesized and evaluated as a novel class of multi-targeting agents to treat Alzheimer's disease (AD). The biological assay results demonstrate the ability of several ... ...

Abstract	A library of fifty-seven 2,4-disubstituted quinazoline derivatives were designed, synthesized and evaluated as a novel class of multi-targeting agents to treat Alzheimer's disease (AD). The biological assay results demonstrate the ability of several quinazoline derivatives to inhibit both acetyl and butyrylcholinesterase (AChE and BuChE) enzymes (IC
MeSH term(s)	Amyloid beta-Peptides/chemistry ; Antioxidants/chemistry ; Antioxidants/metabolism ; Antioxidants/pharmacology ; Butyrylcholinesterase/chemistry ; Butyrylcholinesterase/metabolism ; Cholinesterase Inhibitors/chemistry ; Cholinesterase Inhibitors/metabolism ; Cholinesterase Inhibitors/pharmacology ; Drug Design ; Humans ; Molecular Docking Simulation ; Peptide Fragments/chemistry ; Protein Aggregates/drug effects ; Protein Conformation ; Quinazolines/chemistry ; Quinazolines/metabolism ; Quinazolines/pharmacology ; Structure-Activity Relationship
Chemical Substances	Amyloid beta-Peptides ; Antioxidants ; Cholinesterase Inhibitors ; Peptide Fragments ; Protein Aggregates ; Quinazolines ; amyloid beta-protein (1-40) ; amyloid beta-protein (1-42) ; Butyrylcholinesterase (EC 3.1.1.8)
Language	English
Publishing date	2017-01-27
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.2016.12.005
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Article ; Online: Tau Derived Hexapeptide AcPHF6 Promotes Beta-Amyloid (Aβ) Fibrillogenesis.

Mohamed, Tarek / Gujral, Sarbjeet Singh / Rao, Praveen P N

ACS chemical neuroscience

2017 Volume 9, Issue 4, Page(s) 773–782

Abstract: We studied the interactions of a tau derived hexapeptide AcPHF6 with β-amyloid peptides Aβ40 and Aβ42 which reveals its unusual ability to promote Aβ fibrillogenesis. The results demonstrate that the N-acetylated and C-amidated AcPHF6 hexapeptide can ... ...

Abstract	We studied the interactions of a tau derived hexapeptide AcPHF6 with β-amyloid peptides Aβ40 and Aβ42 which reveals its unusual ability to promote Aβ fibrillogenesis. The results demonstrate that the N-acetylated and C-amidated AcPHF6 hexapeptide can cause significant acceleration in Aβ40 and Aβ42 fibril growth. Aggregation kinetic studies at pH 7.4 show that at 25 μM, AcPHF6 hexapeptide was able to cause ∼2.3-fold increase in Aβ40 fibrillogenesis dramatically changing the aggregation kinetics. In addition, AcPHF6 peptide was able to reduce cellular toxicity mediated by Aβ40 and Aβ42 in hippocampal neuronal cell line (HT22). Computational studies suggest that the AcPHF6 peptide can act as an anchor and provides a hydrophobic surface for Aβ monomer to bind and undergo rapid fibrillogenesis to form less toxic fibrils and alter the aggregation kinetics. At the molecular level we propose a "dock-and-pack" mechanism where the AcPHF6 hexapeptide aggregates can stabilize the β-hairpin and promote rapid Aβ self-assembly and growth to form less toxic oligomers or fibrils. Our results have direct implications in designing novel peptide/peptidomimetics as novel pharmacological tools to study protein aggregation and potentially prevent Aβ-mediated toxicity in Alzheimer's disease.
MeSH term(s)	Alzheimer Disease/drug therapy ; Alzheimer Disease/metabolism ; Amyloid/drug effects ; Amyloid/metabolism ; Amyloid beta-Peptides/metabolism ; Cell Line ; Humans ; Hydrophobic and Hydrophilic Interactions/drug effects ; Neurons/drug effects ; Oligopeptides/chemistry ; Oligopeptides/pharmacology
Chemical Substances	Amyloid ; Amyloid beta-Peptides ; Oligopeptides ; acetyl-valyl-glutaminyl-isoleucyl-valyl-tyrosyl-lysinamide
Language	English
Publishing date	2017-12-27
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	1948-7193
ISSN (online)	1948-7193
DOI	10.1021/acschemneuro.7b00433
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Article ; Online: Interactions of polyunsaturated fatty acids with amyloid peptides Aβ40 and Aβ42.

El Shatshat, Amna / Pham, Amy Trinh / Rao, Praveen P N

Archives of biochemistry and biophysics

2018 Volume 663, Page(s) 34–43

Abstract: Polyunsaturated fatty acids (PUFAs) are reported to exert beneficial effects in Alzheimer's disease. Some PUFAs are known to reduce amyloid-beta (Aβ) toxicity by promoting its degradation and clearance. Studies on the direct interactions of PUFAs with Aβ ...

Abstract	Polyunsaturated fatty acids (PUFAs) are reported to exert beneficial effects in Alzheimer's disease. Some PUFAs are known to reduce amyloid-beta (Aβ) toxicity by promoting its degradation and clearance. Studies on the direct interactions of PUFAs with Aβ peptides are limited and contradictory. In this study, we report the interactions of fatty acids docosahexaenoic acid (DHA), eicosatetraenoic acid (EPA), α-linolenic acid (ALA), arachidonic acid (ARA), linoleic acid (LNA) and oleic acid (OA) with Aβ peptides by carrying out fluorescence based aggregation kinetic experiments, transmission electron microscopy and molecular docking studies. Our investigations demonstrate that all the fatty acids tested exhibit anti-aggregation properties by preventing both Aβ40 and Aβ42 fibrillogenesis (∼16-84% inhibition). OA and DHA were identified as excellent inhibitors of Aβ40 or Aβ42 fibrillogenesis respectively (∼84% and 81% inhibition at 25 μM). Molecular docking studies conducted, using the dimer and oligomer models of Aβ40 peptide, suggest that these fatty acids interact in the aggregation prone Phe19-Ala21 and the β-turn region (Asp23-Lys28) whereas a similar study with Aβ42 dimer and oligomer models, indicate that the fatty acids were oriented in a hydrophobic region (Gln15, Leu16, Leu17 and Leu34). These results, suggest that DHA, EPA, ALA, ARA, LNA and OA are capable of directly interacting with both Aβ40 and Aβ42 peptides. These studies will have implications in developing potential therapeutics for Alzheimer's disease.
MeSH term(s)	Amyloid beta-Peptides/metabolism ; Dimerization ; Fatty Acids, Unsaturated/metabolism ; Humans ; Kinetics ; Microscopy, Electron, Transmission ; Molecular Docking Simulation ; Peptide Fragments/metabolism ; Protein Binding ; Spectrometry, Fluorescence
Chemical Substances	Amyloid beta-Peptides ; Fatty Acids, Unsaturated ; Peptide Fragments ; amyloid beta-protein (1-40) ; amyloid beta-protein (1-42)
Language	English
Publishing date	2018-12-26
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	523-x
ISSN	1096-0384 ; 0003-9861
ISSN (online)	1096-0384
ISSN	0003-9861
DOI	10.1016/j.abb.2018.12.027
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Article: Drug Repurposing: Dipeptidyl Peptidase IV (DPP4) Inhibitors as Potential Agents to Treat SARS-CoV-2 (2019-nCoV) Infection.

Rao, Praveen P N / Pham, Amy Trinh / Shakeri, Arash / El Shatshat, Amna / Zhao, Yusheng / Karuturi, Rahul C / Hefny, Ahmed A

Pharmaceuticals (Basel, Switzerland)

2021 Volume 14, Issue 1

Abstract: The current outbreak of severe acute respiratory distress syndrome (SARS) or nCOVID-19 pandemic, caused by the coronavirus-2 (CoV-2), continues to wreak havoc globally. As novel vaccines are being discovered and developed, small molecule drugs still ... ...

Abstract	The current outbreak of severe acute respiratory distress syndrome (SARS) or nCOVID-19 pandemic, caused by the coronavirus-2 (CoV-2), continues to wreak havoc globally. As novel vaccines are being discovered and developed, small molecule drugs still constitute a viable treatment option for SARS-CoV-2 infections due to their advantages such as superior patient compliance for oral therapies, reduced manufacturing costs and ease of large scale distribution due to better stability and storage profiles. Discovering new drugs for SARS-CoV-2 infections is a time consuming and expensive proposition. In this regard, drug repurposing is an appealing approach which can provide rapid access to therapeutics with proven record of safety and efficacy. We investigated the drug repurposing potential of a library of dipeptidyl peptidase 4 (DPP4) inhibitors which are currently marketed for type-2 diabetes as treatment option for SARS-CoV-2 infections. These computational studies led to the identification of three marketed DPP4 inhibitors; gemigliptin, linagliptin and evogliptin as potential inhibitors of SARS-CoV-2 M
Language	English
Publishing date	2021-01-08
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	2193542-7
ISSN	1424-8247
ISSN	1424-8247
DOI	10.3390/ph14010044
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