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  1. Article ; Online: HDAC Inhibition as Neuroprotection in COVID-19 Infection.

    Sixto-López, Yudibeth / Correa-Basurto, José

    Current topics in medicinal chemistry

    2022  Volume 22, Issue 16, Page(s) 1369–1378

    Abstract: The SARS-CoV-2 virus is responsible for COVID-19 affecting millions of humans around the world. COVID-19 shows various clinical symptoms (fever, cough, fatigue, diarrhea, body aches, headaches, anosmia, and hyposmia). Approximately 30% of patients with ... ...

    Abstract The SARS-CoV-2 virus is responsible for COVID-19 affecting millions of humans around the world. COVID-19 shows various clinical symptoms (fever, cough, fatigue, diarrhea, body aches, headaches, anosmia, and hyposmia). Approximately 30% of patients with COVID-19 showed neurological symptoms, from mild to severe manifestations including headache, dizziness, impaired consciousness, encephalopathy, anosmia, hypogeusia, and hyposmia, among others. The neurotropism of the SARS-CoV-2 virus explains its neuroinvasion provoking neurological damage such as acute demyelination, neuroinflammation, etc. At the molecular level, the COVID-19 patients had higher levels of cytokines and chemokines known as cytokines storms which disrupt the blood-brain barrier allowing the entrance of monocytes and lymphocytes, causing neuroinflammation, neurodegeneration, and demyelination. In addition, the proinflammatory cytokines have been observed in ischemic, hemorrhagic strokes, seizures, and encephalopathy. In this sense, early neuroprotective management should be adopted to avoid or decrease neurological damage due to SARS-CoV-2 infection. Several approaches can be used; one of them includes using HDAC inhibitors (HDACi) due to their neuroprotective effects. Also, the HDACi down-regulates the proinflammatory cytokines (IL-6 and TNF-α) decreasing the neurotoxicity. HDACi can also avoid and prevent the entrance of the virus into the central nervous System (CNS) and decrease the virus replication by downregulating the virus receptors. Here we review the mechanisms that could explain how the SARS-CoV-2 virus could reach the CNS, induce neurological damage and symptoms, and the possibility to use HDACi as neuroprotective therapy.
    MeSH term(s) Anosmia ; Brain Diseases ; COVID-19/drug therapy ; Cytokines ; Demyelinating Diseases/complications ; Humans ; Nervous System Diseases ; Neuroprotection ; SARS-CoV-2
    Chemical Substances Cytokines
    Language English
    Publishing date 2022-03-03
    Publishing country United Arab Emirates
    Document type Journal Article ; Review
    ZDB-ID 2064823-6
    ISSN 1873-4294 ; 1568-0266
    ISSN (online) 1873-4294
    ISSN 1568-0266
    DOI 10.2174/1568026622666220303113445
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Drug repositioning to target NSP15 protein on SARS-CoV-2 as possible COVID-19 treatment.

    Sixto-López, Yudibeth / Martínez-Archundia, Marlet

    Journal of computational chemistry

    2021  Volume 42, Issue 13, Page(s) 897–907

    Abstract: SARS-CoV and SARS-CoV-2 belong to the subfamily Coronaviridae and infect humans, they are constituted by four structural proteins: Spike glycoprotein (S), membrane (M), envelope (E) and nucleocapsid (N), and nonstructural proteins, such as Nsp15 protein ... ...

    Abstract SARS-CoV and SARS-CoV-2 belong to the subfamily Coronaviridae and infect humans, they are constituted by four structural proteins: Spike glycoprotein (S), membrane (M), envelope (E) and nucleocapsid (N), and nonstructural proteins, such as Nsp15 protein which is exclusively present on nidoviruses and is absent in other RNA viruses, making it an ideal target in the field of drug design. A virtual screening strategy to search for potential drugs was proposed, using molecular docking to explore a library of approved drugs available in the DrugBank database in order to identify possible NSP15 inhibitors to treat Covid19 disease. We found from the docking analysis that the antiviral drugs: Paritaprevir and Elbasvir, currently both approved for hepatitis C treatment which showed some of the lowest free binding energy values were considered as repositioning drugs to combat SARS-CoV-2. Furthermore, molecular dynamics simulations of the Apo and Holo-Nsp15 systems were performed in order to get insights about the stability of these protein-ligand complexes.
    MeSH term(s) Antiviral Agents/pharmacology ; Benzofurans/pharmacology ; COVID-19/virology ; Cyclopropanes/pharmacology ; Drug Repositioning ; Endoribonucleases/antagonists & inhibitors ; Endoribonucleases/metabolism ; Humans ; Imidazoles/pharmacology ; Lactams, Macrocyclic/pharmacology ; Molecular Docking Simulation ; Molecular Targeted Therapy ; Proline/analogs & derivatives ; Proline/pharmacology ; SARS-CoV-2/drug effects ; SARS-CoV-2/metabolism ; Sulfonamides/pharmacology ; Viral Nonstructural Proteins/antagonists & inhibitors ; Viral Nonstructural Proteins/metabolism ; COVID-19 Drug Treatment
    Chemical Substances Antiviral Agents ; Benzofurans ; Cyclopropanes ; Imidazoles ; Lactams, Macrocyclic ; Sulfonamides ; Viral Nonstructural Proteins ; elbasvir (632L571YDK) ; Proline (9DLQ4CIU6V) ; Endoribonucleases (EC 3.1.-) ; nidoviral uridylate-specific endoribonuclease (EC 3.1.-) ; paritaprevir (OU2YM37K86)
    Language English
    Publishing date 2021-03-13
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1479181-X
    ISSN 1096-987X ; 0192-8651
    ISSN (online) 1096-987X
    ISSN 0192-8651
    DOI 10.1002/jcc.26512
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article ; Online: Design and simulation of a caprylic acid enzymatically modified phosphatidylcholine micelle using a coarse-grained molecular dynamics simulations approach.

    Santos-Luna, Dalia / Sixto-López, Yudibeth / Bravo-Alfaro, Diego / Cano-Sarmiento, Cynthia / García, Hugo / Correa-Basurto, José

    Journal of biomolecular structure & dynamics

    2023  Volume 41, Issue 23, Page(s) 13902–13913

    Abstract: Computationally simulated micelle models provide useful structural information on the molecular and biological sciences. One strategy to study the self-aggregation process of surfactant molecules that make up a micelle is through molecular dynamics (MD) ... ...

    Abstract Computationally simulated micelle models provide useful structural information on the molecular and biological sciences. One strategy to study the self-aggregation process of surfactant molecules that make up a micelle is through molecular dynamics (MD) simulations. In this study, a theoretical approach with a coarse-grained MD simulation (CG-MD) was employed to evaluate the critical micellar concentration (CMC), the micellization process, building a tridimensional (3D) model system of a micelle using data from the experimentally enzymatically modified phospholipids (PL) by phospholipase A1 (PA1). This required enzymatic interesterification of soybean phosphatidylcholine (PC) with caprylic acid, along with purification and characterization by chromatographic techniques to measure the esterified fatty acids and the corresponding PL composition. The number of molecules used in the CG-MD simulation system was determined from the experimental CMC data which was 0.025%. The molecular composition of the system is:
    MeSH term(s) Molecular Dynamics Simulation ; Micelles ; Caprylates ; Phosphatidylcholines
    Chemical Substances Micelles ; octanoic acid (OBL58JN025) ; Caprylates ; Phosphatidylcholines
    Language English
    Publishing date 2023-02-24
    Publishing country England
    Document type Journal Article
    ZDB-ID 49157-3
    ISSN 1538-0254 ; 0739-1102
    ISSN (online) 1538-0254
    ISSN 0739-1102
    DOI 10.1080/07391102.2023.2180434
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article ; Online: Exploring the inhibitory activity of valproic acid against the HDAC family using an MMGBSA approach.

    Sixto-López, Yudibeth / Bello, Martiniano / Correa-Basurto, José

    Journal of computer-aided molecular design

    2020  Volume 34, Issue 8, Page(s) 857–878

    Abstract: Valproic acid (VPA) is a compound currently used in clinical practice for the treatment of epilepsy as well as bipolar and mood disorders. VPA targets histone deacetylases (HDACs), which participate in the removal of acetyl groups from lysine in several ... ...

    Abstract Valproic acid (VPA) is a compound currently used in clinical practice for the treatment of epilepsy as well as bipolar and mood disorders. VPA targets histone deacetylases (HDACs), which participate in the removal of acetyl groups from lysine in several proteins, regulating a wide variety of functions within the organism. An imbalance or malfunction of these enzymes is associated with the development and progression of several diseases, such as cancer and neurodegenerative diseases. HDACs are divided into four classes, but VPA only targets Class I (HDAC1-3 and 8) and Class IIa (HDAC4-5, 7 and 9) HDACs; however, structural and energetic information regarding the manner by which VPA inhibits these HDACs is lacking. Here, the structural and energetic features that determine this recognition were studied using molecular docking and molecular dynamics (MD) simulation. It was found that VPA reaches the catalytic site in HDAC1-3 and 7, whereas in HDAC6, VPA only reaches the catalytic tunnel. In HDAC4, VPA was bound adjacent to L1 and L2, a zone that participates in corepressor binding, and in HDAC8, VPA was bound to the hydrophobic active site channel (HASC), in line with previous reports.
    MeSH term(s) Crystallography, X-Ray ; Histone Deacetylase 1/chemistry ; Histone Deacetylase 1/metabolism ; Histone Deacetylase 6/chemistry ; Histone Deacetylase 6/metabolism ; Histone Deacetylase Inhibitors/chemistry ; Histone Deacetylase Inhibitors/pharmacology ; Humans ; Molecular Docking Simulation/methods ; Molecular Dynamics Simulation ; Principal Component Analysis ; Protein Conformation ; Reproducibility of Results ; Valproic Acid/chemistry ; Valproic Acid/pharmacology
    Chemical Substances Histone Deacetylase Inhibitors ; Valproic Acid (614OI1Z5WI) ; HDAC1 protein, human (EC 3.5.1.98) ; HDAC6 protein, human (EC 3.5.1.98) ; Histone Deacetylase 1 (EC 3.5.1.98) ; Histone Deacetylase 6 (EC 3.5.1.98)
    Language English
    Publishing date 2020-03-16
    Publishing country Netherlands
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 808166-9
    ISSN 1573-4951 ; 0920-654X
    ISSN (online) 1573-4951
    ISSN 0920-654X
    DOI 10.1007/s10822-020-00304-2
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article ; Online: Cytotoxic evaluation of YSL-109 in a triple negative breast cancer cell line and toxicological evaluations.

    Sixto-López, Yudibeth / Ordaz-Pichardo, Cynthia / Gómez-Vidal, José Antonio / Rosales-Hernández, Martha Cecilia / Correa-Basurto, José

    Naunyn-Schmiedeberg's archives of pharmacology

    2023  Volume 396, Issue 6, Page(s) 1211–1222

    Abstract: Breast cancer (BC) is the leading cause of cancer-related death in women worldwide. Triple negative breast cancer (TNBC) is the most aggressive form of BC being with the worst prognosis and the worst survival rates. There is no specific pharmacological ... ...

    Abstract Breast cancer (BC) is the leading cause of cancer-related death in women worldwide. Triple negative breast cancer (TNBC) is the most aggressive form of BC being with the worst prognosis and the worst survival rates. There is no specific pharmacological target for the treatment of TNBC; conventional therapy includes the use of non-specific chemotherapy that generally has a poor prognosis. Therefore, the search of effective therapies against to TNBC continues at both preclinical and clinical level. In this sense, the exploration of different pharmacological targets is a continue task that pave the way to epigenetic modulation using novel small molecules. Lately, the inhibition of histone deacetylases (HDACs) has been explored to treat different BC, including TNBC. HDACs remove the acetyl groups from the ɛ-amino lysine resides on histone and non-histone proteins. In particular, the inhibition of HDAC6 has been suggested to be useful for the treatment of TNBC due to it is overexpressed in TNBC. Therefore, in this work, an HDAC6 selective inhibitor, the (S)-4-butyl-N-(1-(hydroxyamino)-3-(naphthalen-1-yl)-1-oxopropan-2-yl) benzamide (YSL-109), was assayed on TNBC cell line (MDA-MB231) showing an antiproliferative activity (IC
    MeSH term(s) Humans ; Female ; Animals ; Mice ; Triple Negative Breast Neoplasms/drug therapy ; Triple Negative Breast Neoplasms/metabolism ; Histone Deacetylase Inhibitors ; Cell Line, Tumor ; Cell Proliferation ; Antineoplastic Agents/pharmacology ; Antineoplastic Agents/therapeutic use
    Chemical Substances Histone Deacetylase Inhibitors ; Antineoplastic Agents
    Language English
    Publishing date 2023-01-25
    Publishing country Germany
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 121471-8
    ISSN 1432-1912 ; 0028-1298
    ISSN (online) 1432-1912
    ISSN 0028-1298
    DOI 10.1007/s00210-023-02396-7
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article ; Online: Computational study of DMPC liposomes loaded with the N-(2-Hydroxyphenyl)-2-propylpentanamide (HO-AAVPA) and determination of its antiproliferative activity

    Marcos, Xelhua / Sixto-López, Yudibeth / Pérez-Casas, Silvia / Correa-Basurto, José

    Journal of biomolecular structure & dynamics

    2021  Volume 40, Issue 21, Page(s) 11448–11459

    Abstract: ... ...

    Abstract N
    MeSH term(s) Mice ; Animals ; Dimyristoylphosphatidylcholine/chemistry ; Dimyristoylphosphatidylcholine/metabolism ; Liposomes/chemistry ; NIH 3T3 Cells ; Lipid Bilayers/chemistry ; Cholesterol/chemistry ; Water
    Chemical Substances Dimyristoylphosphatidylcholine (U86ZGC74V5) ; Liposomes ; N-(2-hydroxyphenyl)-2-propylpentanamide ; Lipid Bilayers ; Cholesterol (97C5T2UQ7J) ; Water (059QF0KO0R)
    Language English
    Publishing date 2021-07-27
    Publishing country England
    Document type Journal Article ; Review ; Research Support, Non-U.S. Gov't
    ZDB-ID 49157-3
    ISSN 1538-0254 ; 0739-1102
    ISSN (online) 1538-0254
    ISSN 0739-1102
    DOI 10.1080/07391102.2021.1955744
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  7. Article ; Online: Structural and energetic basis for the inhibitory selectivity of both catalytic domains of dimeric HDAC6.

    Sixto-López, Yudibeth / Bello, Martiniano / Correa-Basurto, José

    Journal of biomolecular structure & dynamics

    2019  Volume 37, Issue 18, Page(s) 4701–4720

    Abstract: HDAC6 is a protein involved in cancer, neurodegenerative disease and inflammatory disorders. To date, the full three-dimensional (3D) structure of human HDAC6 has not been elucidated; however, there are some experimental 3D structural homologs to HDAC6 ... ...

    Abstract HDAC6 is a protein involved in cancer, neurodegenerative disease and inflammatory disorders. To date, the full three-dimensional (3D) structure of human HDAC6 has not been elucidated; however, there are some experimental 3D structural homologs to HDAC6 that can be used as templates. In this work, we utilized molecular modeling procedures to model both of the catalytic domains of HDAC6 connected by the linker region where DMB region is placed. Once the 3D structure of human HDAC6 was obtained, it was structurally evaluated and submitted to docking and molecular dynamic (MD) simulations along with Molecular Mechanics/Generalized Born Surface Area (MM/GBSA) method to explore the stability and the binding free energy properties of the HDAC6-ligand complexes. In addition, its structural and energetic behavior was explored with each one of the catalytic domains in the molecular recognition of six selective HDAC6 inhibitors, HPOB, CAY10603, Nexturastat, Rocilinostat, Tubacin and Tubastatin A for DD2, and with the so-called 9-peptide which is DD1-HDAC6 selective substrate. The use of the whole system (DD1-DMB-DD2) showed a tendency toward the ligand affinity of DD2, CAY10603> Tubacin > Rocilinostat > Nexturastat > HPOB > Tubastatin > 9-peptide, which is in line with experimental reports. However, 9-peptide showed a higher affinity for DD1, which agrees with experimental reports elsewhere. Principal component analysis provided important information about the structural changes linked to the molecular recognition process, whereas per-residue decomposition analysis revealed the energetic contribution of the key residues in the molecular binding and structural characteristics that could assist in drug design.
    MeSH term(s) Anilides/chemistry ; Carbamates/chemistry ; Catalytic Domain/genetics ; Cluster Analysis ; Histone Deacetylase 6/antagonists & inhibitors ; Histone Deacetylase 6/chemistry ; Histone Deacetylase 6/genetics ; Histone Deacetylase Inhibitors/chemistry ; Humans ; Hydroxamic Acids/chemistry ; Indoles/chemistry ; Ligands ; Molecular Docking Simulation ; Molecular Dynamics Simulation ; Oxazoles/chemistry ; Phenylurea Compounds/chemistry ; Principal Component Analysis ; Pyrimidines/chemistry ; Structure-Activity Relationship
    Chemical Substances 4-((1-butyl-3-phenylureido)methyl)-N-hydroxybenzamide ; Anilides ; CAY10603 ; Carbamates ; Histone Deacetylase Inhibitors ; Hydroxamic Acids ; Indoles ; Ligands ; Oxazoles ; Phenylurea Compounds ; Pyrimidines ; tubacin (02C2G1D30D) ; tubastatin A (2XTSOX1NF8) ; HDAC6 protein, human (EC 3.5.1.98) ; Histone Deacetylase 6 (EC 3.5.1.98) ; ricolinostat (WKT909C62B)
    Language English
    Publishing date 2019-02-10
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 49157-3
    ISSN 1538-0254 ; 0739-1102
    ISSN (online) 1538-0254
    ISSN 0739-1102
    DOI 10.1080/07391102.2018.1557560
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  8. Article ; Online: Insights into structural features of HDAC1 and its selectivity inhibition elucidated by Molecular dynamic simulation and Molecular Docking.

    Sixto-López, Yudibeth / Bello, Martiniano / Correa-Basurto, José

    Journal of biomolecular structure & dynamics

    2018  Volume 37, Issue 3, Page(s) 584–610

    Abstract: Histone deacetylases (HDACs) are a family of proteins whose main function is the removal of acetyl groups from lysine residues located on histone and non-histone substrates, which regulates gene transcription and other activities in cells. HDAC1 ... ...

    Abstract Histone deacetylases (HDACs) are a family of proteins whose main function is the removal of acetyl groups from lysine residues located on histone and non-histone substrates, which regulates gene transcription and other activities in cells. HDAC1 dysfunction has been implicated in cancer development and progression; thus, its inhibition has emerged as a new therapeutic strategy. Two additional metal binding sites (Site 1 and Site 2) in HDACs have been described that are primarily occupied by potassium ions, suggesting a possible structural role that affects HDAC activity. In this work, we explored the structural role of potassium ions in Site 1 and Site 2 and how they affect the interactions of compounds with high affinities for HDAC1 (AC1OCG0B, Chlamydocin, Dacinostat and Quisinostat) and SAHA (a pan-inhibitor) using molecular docking and molecular dynamics (MD) simulations in concert with a Molecular-Mechanics-Generalized-Born-Surface-Area (MMGBSA) approach. Four models were generated: one with a potassium ion (K
    MeSH term(s) Amino Acid Sequence ; Binding Sites ; Drug Design ; Histone Deacetylase 1/antagonists & inhibitors ; Histone Deacetylase 1/chemistry ; Histone Deacetylase Inhibitors/chemistry ; Histone Deacetylase Inhibitors/pharmacology ; Inhibitory Concentration 50 ; Ligands ; Molecular Docking Simulation ; Molecular Dynamics Simulation ; Thermodynamics
    Chemical Substances Histone Deacetylase Inhibitors ; Ligands ; Histone Deacetylase 1 (EC 3.5.1.98)
    Language English
    Publishing date 2018-03-06
    Publishing country England
    Document type Journal Article
    ZDB-ID 49157-3
    ISSN 1538-0254 ; 0739-1102
    ISSN (online) 1538-0254
    ISSN 0739-1102
    DOI 10.1080/07391102.2018.1441072
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  9. Article ; Online: Molecular insight into endosulfan degradation by Ese protein from Arthrobacter: Evidence-based structural bioinformatics and quantum mechanical calculations.

    Andrade-Collantes, Ernesto / Landeros-Rivera, Bruno / Sixto-López, Yudibeth / Bello-Rios, Ciresthel / Contreras-García, Julia / Tiznado, José Antonio Garzón / Pedroza-Torres, Abraham / Camacho-Pérez, Beni / Montaño, Sarita

    Proteins

    2023  Volume 92, Issue 2, Page(s) 302–313

    Abstract: Endosulfan is an organochlorine insecticide widely used for agricultural pest control. Many nations worldwide have restricted or completely banned it due to its extreme toxicity to fish and aquatic invertebrates. Arthrobacter sp. strain KW has the ... ...

    Abstract Endosulfan is an organochlorine insecticide widely used for agricultural pest control. Many nations worldwide have restricted or completely banned it due to its extreme toxicity to fish and aquatic invertebrates. Arthrobacter sp. strain KW has the ability to degrade α, β endosulfan and its intermediate metabolite endosulfate; this degradation is associated with Ese protein, a two-component flavin-dependent monooxygenase (TC-FDM). Employing in silico tools, we obtained the 3D model of Ese protein, and our results suggest that it belongs to the Luciferase Like Monooxygenase family (LLM). Docking studies showed that the residues V59, V315, D316, and T335 interact with α-endosulfan. The residues: V59, T60, V315, D316, and T335 are implicated in the interacting site with β-endosulfan, and the residues: H17, V315, D316, T335, N364, and Q363 participate in the interaction with endosulfate. Topological analysis of the electron density by means of the Quantum Theory of Atoms in Molecules (QTAIM) and the Non-Covalent Interaction (NCI) index reveals that the Ese-ligands complexes are formed mainly by dispersive forces, where Cl atoms have a predominant role. As Ese is a monooxygenase member, we predict the homodimer formation. However, enzymatic studies must be developed to investigate the Ese protein's enzymatic and catalytic activity.
    MeSH term(s) Animals ; Endosulfan/chemistry ; Endosulfan/metabolism ; Arthrobacter/metabolism ; Biodegradation, Environmental ; Insecticides/chemistry ; Insecticides/metabolism ; Mixed Function Oxygenases
    Chemical Substances Endosulfan (OKA6A6ZD4K) ; Insecticides ; Mixed Function Oxygenases (EC 1.-)
    Language English
    Publishing date 2023-10-20
    Publishing country United States
    Document type Journal Article
    ZDB-ID 806683-8
    ISSN 1097-0134 ; 0887-3585
    ISSN (online) 1097-0134
    ISSN 0887-3585
    DOI 10.1002/prot.26610
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  10. Article ; Online: In silico design of HDAC6 inhibitors with neuroprotective effects.

    Sixto-López, Yudibeth / Gómez-Vidal, José Antonio / de Pedro, Nuria / Bello, Martiniano / Rosales-Hernández, Martha Cecilia / Correa-Basurto, José

    Journal of biomolecular structure & dynamics

    2021  Volume 40, Issue 24, Page(s) 14204–14222

    Abstract: HDAC6 has emerged as a molecular target to treat neurodegenerative disorders, due to its participation in protein aggregate degradation, oxidative stress process, mitochondrial transport, and axonal transport. Thus, in this work we have designed a set of ...

    Abstract HDAC6 has emerged as a molecular target to treat neurodegenerative disorders, due to its participation in protein aggregate degradation, oxidative stress process, mitochondrial transport, and axonal transport. Thus, in this work we have designed a set of 485 compounds with hydroxamic and bulky-hydrophobic moieties that may function as HDAC6 inhibitors with a neuroprotective effect. These compounds were filtered by their predicted ADMET properties and their affinity to HDAC6 demonstrated by molecular docking and molecular dynamics simulations. The combination of
    MeSH term(s) Neuroprotective Agents/pharmacology ; Histone Deacetylase 6/chemistry ; Molecular Docking Simulation ; Molecular Dynamics Simulation ; Histone Deacetylase Inhibitors/pharmacology ; Histone Deacetylase Inhibitors/chemistry ; Hydroxamic Acids/pharmacology ; Hydroxamic Acids/chemistry
    Chemical Substances Neuroprotective Agents ; Histone Deacetylase 6 (EC 3.5.1.98) ; Histone Deacetylase Inhibitors ; Hydroxamic Acids
    Language English
    Publishing date 2021-11-16
    Publishing country England
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 49157-3
    ISSN 1538-0254 ; 0739-1102
    ISSN (online) 1538-0254
    ISSN 0739-1102
    DOI 10.1080/07391102.2021.2001378
    Database MEDical Literature Analysis and Retrieval System OnLINE

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