Karina de Carvalho Pougy

@ppgbq.iq.ufrj.br

MSc. Department of Biochemistry
Post-Graduate Program in Biochemistry

Karina de Carvalho Pougy


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https://researchid.co/karipougy

EDUCATION

Master in Science by the Biochemistry Post-graduation Program from he Federal University of Rio de Janeiro (UFRJ). Chemist by UFRJ.

PhD student at UFRJ.

RESEARCH, TEACHING, or OTHER INTERESTS

Molecular Biology, Biophysics, Biochemistry, Biotechnology
7

Scopus Publications

113

Scholar Citations

5

Scholar h-index

3

Scholar i10-index

Scopus Publications

  • Differential Modulation of Copper(II) Interactions with the 18–22 Coordinating Amylin Fragment by the Geometric Isomers of a New Nicotinoyl Hydrazone: A First Study
    Alessandra Carvalho, Karina C. Pougy, Anderson S. Pinheiro, Daphne S. Cukierman, Nicolás A. Rey
    ACS Omega, 2025
    High Resolution Image Download MS PowerPoint Slide Type 2 diabetes mellitus is a multifactorial disease associated with insulin resistance and pancreatic β-cell dysfunction. Interestingly, this disease has also been associated with the aggregation of islet amyloid polypeptide (IAPP or amylin). This peptide can bind to physiological metal ions such as copper(II), which enhances its aggregation and induces oxidative stress. For this reason, the use of moderate chelators constitutes a compelling potential therapeutic strategy. In this work, we synthesized and characterized the geometric isomers of a new compound, 1-methylimidazole-2-carboxaldehyde nicotinoyl hydrazone ( X1NIC ), aiming to evaluate their differential interactions with copper(II) and the hIAPP 18–22 peptide fragment. Both compounds demonstrated high aqueous stability and adequate lipophilicity for biological membrane crossing. Coordination studies revealed that both ML and ML 2 complexes can be obtained in solution for the tridentate ligand X1NIC-( E ), with the former being more stable. On the other hand, the bidentate ligand X1NIC-( Z ) only forms ML species. Both isomers effectively set up ternary complexes with Cu 2+ and hIAPP 18–22, altering the redox behavior of the copper-peptide system. These results, obtained through cyclic voltammetry experiments, suggest a protective effect of the ligands with respect to metal-induced oxidative stress. This study constitutes the first comparative report on the coordination and reactivity of geometric isomers of a bioactive N -acylhydrazone, and the findings described herein highlight this class of compounds as promising chemical tools for the modulation of abnormal metal-peptide interactions implicated in type 2 diabetes pathogenesis.
  • Phase separation as a key mechanism in plant development, environmental adaptation, and abiotic stress response
    Karina C. Pougy, Bruna A. Brito, Giovanna S. Melo, Anderson S. Pinheiro
    Journal of Biological Chemistry, 2025
    In memoriam of Professor Anderson de Sá Pinheiro, principal investigator at the Laboratory of Molecular Biology (LabMol) at the Institute of Chemistry, Federal University of Rio de Janeiro (UFRJ). Prof. Pinheiro passed away prematurely at the age of 44, on March 1, 2025. Prof. Pinheiro was a distinguished figure in the fields of biochemistry and structural biology in Brazil. He earned his bachelor's degree in Pharmacy in 2000, his master's degree in 2003, and his Ph.D. in 2007, all in Biological Chemistry at UFRJ. He continued his academic journey with postdoctoral research at Brown University in the United States (2007-2011). Upon returning to Brazil, he became an Associate Professor in the Department of Biochemistry at UFRJ (2011-2025). He led the Laboratory of Molecular Biochemistry (LaBMol), focusing on the study of RNA-binding proteins related to cancer and neurodegenerative disorders, as well as plant responses to abiotic stress. His research followed two main fronts-analyzing protein structures and dynamics using solution NMR spectroscopy and investigating the relationship between structural features and liquid-liquid phase separation, along with its role in protein function. Beyond research, Prof. Anderson was deeply committed to education, mentoring numerous students and contributing to various academic committees. During his brief but impactful career, he made significant contributions to the structural biology community, serving as President of the Brazilian Association of Nuclear Magnetic Resonance Users (AUREMN) and as Scientific Director of the Brazilian Biophysical Society (SBBf). This review marks Professor Pinheiro's 50th published article. His untimely passing is a profound loss to the scientific community, but his legacy endures through his scientific contributions and the many lives he has touched. Liquid-liquid phase separation is a fundamental biophysical process in which biopolymers, such as proteins, nucleic acids, and their complexes, spontaneously demix into distinct coexisting phases. This phenomenon drives the formation of membraneless organelles-cellular subcompartments without a lipid bilayer that perform specialized functions. In plants, phase-separated biomolecular condensates play pivotal roles in regulating gene expression, from genome organization to transcriptional and post-transcriptional processes. In addition, phase separation governs plant-specific traits, such as flowering and photosynthesis. As sessile organisms, plants have evolved to leverage phase separation for rapid sensing and response to environmental fluctuations and stress conditions. Recent studies highlight the critical role of phase separation in plant adaptation, particularly in response to abiotic stress. This review compiles the latest research on biomolecular condensates in plant biology, providing examples of their diverse functions in development, environmental adaptation, and stress responses. We propose that phase separation represents a conserved and dynamic mechanism enabling plants to adapt efficiently to ever-changing environmental conditions. Deciphering the molecular mechanisms underlying phase separation in plant stress responses opens new avenues for biotechnological strategies aimed at engineering stress-resistant crops. These advancements have significant implications for agriculture, particularly in addressing crop productivity in the face of climate change.
  • Structural basis of nucleic acid recognition by the N-terminal cold shock domain of the plant glycine-rich protein AtGRP2
    Karina C. Pougy, Beatriz S. Moraes, Clara L.F. Malizia-Motta, Luís Maurício T.R. Lima, Gilberto Sachetto-Martins, Fabio C.L. Almeida, Anderson S. Pinheiro
    Journal of Biological Chemistry, 2024
    AtGRP2 is a glycine-rich, RNA-binding protein that plays pivotal roles in abiotic stress response and flowering time regulation in Arabidopsis thaliana . AtGRP2 consists of an N-terminal cold shock domain (CSD) and two C-terminal CCHC-type zinc knuckles interspersed with glycine-rich regions. Here, we investigated the structure, dynamics, and nucleic acid–binding properties of AtGRP2-CSD. The 2D [ 1 H, 15 N] heteronuclear single quantum coherence spectrum of AtGRP2-CSD 1–79 revealed the presence of a partially folded intermediate in equilibrium with the folded state. The addition of 11 residues at the C terminus stabilized the folded conformation. The three-dimensional structure of AtGRP2-CSD 1–90 unveiled a β-barrel composed of five antiparallel β-strands and a 3 10 helical turn, along with an ordered C-terminal extension, a conserved feature in eukaryotic CSDs. Direct contacts between the C-terminal extension and the β3–β4 loop further stabilized the CSD fold. AtGRP2-CSD 1–90 exhibited nucleic acid binding via solvent-exposed residues on strands β2 and β3, as well as the β3–β4 loop, with higher affinity for DNA over RNA, particularly favoring pyrimidine-rich sequences. Furthermore, DNA binding induced rigidity in the β3–β4 loop, evidenced by 15 N-{ 1 H} NOE values. Mutation of residues W17, F26, and F37, in the central β-sheet, completely abolished DNA binding, highlighting the significance of π-stacking interactions in the binding mechanism. These results shed light on the mechanism of nucleic acid recognition employed by AtGRP2, creating a framework for the development of biotechnological strategies aimed at enhancing plant resistance to abiotic stresses.
  • 1 H, 15 N, and 13 C backbone and side chain resonance assignments of the cold shock domain of the Arabidopsis thaliana glycine-rich protein AtGRP2
    Karina C. Pougy, Gilberto Sachetto-Martins, Fabio C. L. Almeida, Anderson S. Pinheiro
    Biomolecular NMR Assignments, 2023
  • Molecular dynamics simulations of aqueous systems of inhibitor candidates for adenosine-5’-phosphosufate reductase
    Talis Uelisson da Silva, Karina de Carvalho Pougy, Magaly Girão Albuquerque, Camilo Henrique da Silva Lima, Sérgio de Paula Machado
    Journal of Biomolecular Structure and Dynamics, 2023
    Molecular dynamics (MD) simulations were used to evaluate some chelating agents as potential candidates to inhibitors for dissimilatory adenosine-5’-phosphosulfate reductase (APSrAB). Molecular docking methods were used to evaluate the best binding modes of these molecules to the enzyme at two binding sites: of the substrate (enzyme active site) by mean the redocking protocol of substrate; and of one of the [Fe4S4]2+ groups by mean of the clusterization protocol. The best docking poses were selected by criteria such as low energy and RMSD (redocking) and the cluster with the higher number of similar poses (clusterization), which were submitted to MD simulations. RMSD, RDF, and hydrogen bonds results revelated that all ligands left the cube site, while in the active site, some ligands remained in their docking region, pointing to the enzyme active site as the best target for the selected ligands. The binding energy results of ligands hydroxamic acid (HXA) and catechol (CAT) showed that they bonded favorably to the enzyme and key residues of the active site contributed significantly to the protein-ligand bind, indicating HAX and CAT may compete with the substrate for interactions with these residues and displaying potential as candidates for experimental studies about APSrAB inhibitors.Communicated by Ramaswamy H. Sarma
  • Development of parameters compatible with the CHARMM36 force field for [Fe4S4]2+ clusters and molecular dynamics simulations of adenosine-5’-phosphosulfate reductase in GROMACS 2019
    Talis Uelisson da Silva, Karina de Carvalho Pougy, Magaly Girão Albuquerque, Camilo Henrique da Silva Lima, Sérgio de Paula Machado
    Journal of Biomolecular Structure and Dynamics, 2022
    DFT calculations were used to obtain parameters compatible with the CHARMM36 force field for iron-sulfur clusters (Fe-S) of the type [Fe4S4]2+ that are coordinated to dissimilatory adenosine-5’-phosphosulfate reductase (APSrAB). Classical molecular dynamics (MD) simulations were performed on two APSrAB systems to validate the parameters and verify the stability of the studied systems. The time analysis of the parameters inserted into the force field was in reasonable agreement with the experimental X-ray diffraction data. The analysis of the time evolution of the studied systems indicated that these systems and, in particular, the clusters in their respective cavities had a good stability and were in agreement with what was observed in previous works. The parameters obtained provide the basis for the study of APSrAB as well as other systems that contain [Fe4S4]2+ through the CHARMM36 force field.
  • Electronic investigation of the effect of substituents on the SOD mimic activity of copper (II) complexes with 8-hydroxyquinoline-derived ligands
    Talis Uelisson da Silva, Karina de Carvalho Pougy, Everton Tomaz da Silva, Camilo Henrique da Silva Lima, Sérgio de Paula Machado
    Journal of Inorganic Biochemistry, 2021

RECENT SCHOLAR PUBLICATIONS

  • Differential Modulation of Copper (II) Interactions with the 18–22 Coordinating Amylin Fragment by the Geometric Isomers of a New Nicotinoyl Hydrazone: A First Study
    A Carvalho, KC Pougy, AS Pinheiro, DS Cukierman, NA Rey
    ACS omega 10 (28), 31115-31127 , 2025
    2025
    Citations: 4
  • Phase separation as a key mechanism in plant development, environmental adaptation, and abiotic stress response
    KC Pougy, BA Brito, GS Melo, AS Pinheiro
    Journal of Biological Chemistry, 108548 , 2025
    2025
    Citations: 8
  • Structural basis of nucleic acid recognition by the N-terminal cold shock domain of the plant glycine-rich protein AtGRP2
    KC Pougy, BS Moraes, CLF Malizia-Motta, LMTR Lima, ...
    Journal of Biological Chemistry 300 (11) , 2024
    2024
    Citations: 1
  • 1 H, 15 N, and 13 C backbone and side chain resonance assignments of the cold shock domain of the Arabidopsis thaliana glycine-rich protein AtGRP2
    KC Pougy, G Sachetto-Martins, FCL Almeida, AS Pinheiro
    Biomolecular NMR Assignments 17 (1), 143-149 , 2023
    2023
    Citations: 2
  • Molecular dynamics simulations of aqueous systems of inhibitor candidates for adenosine-5’-phosphosufate reductase
    TU da Silva, KC Pougy, MG Albuquerque, CHS Lima, SP Machado
    Journal of Biomolecular Structure and Dynamics 41 (6), 2466-2477 , 2023
    2023
    Citations: 7
  • Development of parameters compatible with the CHARMM36 force field for [Fe 4 S 4 ] 2+ clusters and molecular dynamics simulations of adenosine-5 …
    TU da Silva, KC Pougy, MG Albuquerque, CH da Silva Lima, SP Machado
    Journal of Biomolecular Structure and Dynamics 40 (8), 3481-3491 , 2022
    2022
    Citations: 64
  • Molecular modeling of indazole-3-carboxylic acid and its metal complexes (Zn, Ni, Co, Fe and Mn) as NO synthase inhibitors: DFT calculations, docking studies and molecular …
    TU da Silva, ET da Silva, K de Carvalho Pougy, CH da Silva Lima, ...
    Inorganic Chemistry Communications 135, 109120 , 2022
    2022
    Citations: 12
  • Electronic investigation of the effect of substituents on the SOD mimic activity of copper (II) complexes with 8-hydroxyquinoline-derived ligands
    TU da Silva, K de Carvalho Pougy, ET da Silva, CH da Silva Lima, ...
    Journal of Inorganic Biochemistry 217, 111359 , 2021
    2021
    Citations: 10
  • Caracterização estrutural e da interação com DNA do domínio cold-shock da proteína AtGRP2 de Arabidopsis thaliana por Ressonância Magnética Nuclear
    KC Pougy
    Universidade Federal do Rio de Janeiro , 2021
    2021
  • A DFT study of cis-[Ru (NO)(NO2) bpy (dye) 2] n+ complexes as NO donors
    ET da Silva, TU da Silva, K de Carvalho Pougy, RB da Silveira, ...
    Inorganica Chimica Acta 510, 119724 , 2020
    2020
    Citations: 5
  • USE OF THE DENSITY FUNCTIONAL THEORY IN SPIN CROSSOVER ANALYSIS IN INORGANIC CHEMISTRY CLASSES
    KC Pougy, SP Machado
    Química Nova 43, 127-130 , 2020
    2020

MOST CITED SCHOLAR PUBLICATIONS

  • Development of parameters compatible with the CHARMM36 force field for [Fe 4 S 4 ] 2+ clusters and molecular dynamics simulations of adenosine-5 …
    TU da Silva, KC Pougy, MG Albuquerque, CH da Silva Lima, SP Machado
    Journal of Biomolecular Structure and Dynamics 40 (8), 3481-3491 , 2022
    2022
    Citations: 64
  • Molecular modeling of indazole-3-carboxylic acid and its metal complexes (Zn, Ni, Co, Fe and Mn) as NO synthase inhibitors: DFT calculations, docking studies and molecular …
    TU da Silva, ET da Silva, K de Carvalho Pougy, CH da Silva Lima, ...
    Inorganic Chemistry Communications 135, 109120 , 2022
    2022
    Citations: 12
  • Electronic investigation of the effect of substituents on the SOD mimic activity of copper (II) complexes with 8-hydroxyquinoline-derived ligands
    TU da Silva, K de Carvalho Pougy, ET da Silva, CH da Silva Lima, ...
    Journal of Inorganic Biochemistry 217, 111359 , 2021
    2021
    Citations: 10
  • Phase separation as a key mechanism in plant development, environmental adaptation, and abiotic stress response
    KC Pougy, BA Brito, GS Melo, AS Pinheiro
    Journal of Biological Chemistry, 108548 , 2025
    2025
    Citations: 8
  • Molecular dynamics simulations of aqueous systems of inhibitor candidates for adenosine-5’-phosphosufate reductase
    TU da Silva, KC Pougy, MG Albuquerque, CHS Lima, SP Machado
    Journal of Biomolecular Structure and Dynamics 41 (6), 2466-2477 , 2023
    2023
    Citations: 7
  • A DFT study of cis-[Ru (NO)(NO2) bpy (dye) 2] n+ complexes as NO donors
    ET da Silva, TU da Silva, K de Carvalho Pougy, RB da Silveira, ...
    Inorganica Chimica Acta 510, 119724 , 2020
    2020
    Citations: 5
  • Differential Modulation of Copper (II) Interactions with the 18–22 Coordinating Amylin Fragment by the Geometric Isomers of a New Nicotinoyl Hydrazone: A First Study
    A Carvalho, KC Pougy, AS Pinheiro, DS Cukierman, NA Rey
    ACS omega 10 (28), 31115-31127 , 2025
    2025
    Citations: 4
  • 1 H, 15 N, and 13 C backbone and side chain resonance assignments of the cold shock domain of the Arabidopsis thaliana glycine-rich protein AtGRP2
    KC Pougy, G Sachetto-Martins, FCL Almeida, AS Pinheiro
    Biomolecular NMR Assignments 17 (1), 143-149 , 2023
    2023
    Citations: 2
  • Structural basis of nucleic acid recognition by the N-terminal cold shock domain of the plant glycine-rich protein AtGRP2
    KC Pougy, BS Moraes, CLF Malizia-Motta, LMTR Lima, ...
    Journal of Biological Chemistry 300 (11) , 2024
    2024
    Citations: 1
  • Caracterização estrutural e da interação com DNA do domínio cold-shock da proteína AtGRP2 de Arabidopsis thaliana por Ressonância Magnética Nuclear
    KC Pougy
    Universidade Federal do Rio de Janeiro , 2021
    2021
  • USE OF THE DENSITY FUNCTIONAL THEORY IN SPIN CROSSOVER ANALYSIS IN INORGANIC CHEMISTRY CLASSES
    KC Pougy, SP Machado
    Química Nova 43, 127-130 , 2020
    2020