M. Florencia Martini

ORCID: 0000-0002-1949-9310
Publications
Citations
Views
---
Saved
---
About
Contact & Profiles
Research Areas
  • Lipid Membrane Structure and Behavior
  • Spectroscopy and Quantum Chemical Studies
  • Antimicrobial Peptides and Activities
  • Protein Structure and Dynamics
  • Enzyme Structure and Function
  • Crystallization and Solubility Studies
  • Protein Interaction Studies and Fluorescence Analysis
  • Synthesis and Biological Evaluation
  • Amino Acid Enzymes and Metabolism
  • Biochemical and Molecular Research
  • X-ray Diffraction in Crystallography
  • Surfactants and Colloidal Systems
  • Metabolism and Genetic Disorders
  • Bioactive Compounds and Antitumor Agents
  • Plant biochemistry and biosynthesis
  • Electrochemical sensors and biosensors
  • Trace Elements in Health
  • Metal-Catalyzed Oxygenation Mechanisms
  • Trypanosoma species research and implications
  • Drug Solubulity and Delivery Systems
  • Sphingolipid Metabolism and Signaling
  • Bacteriophages and microbial interactions
  • Electrochemical Analysis and Applications
  • Fluorine in Organic Chemistry
  • Lipid metabolism and biosynthesis

Consejo Nacional de Investigaciones Científicas y Técnicas
2015-2024

Buenos Aires Institute of Technology
2024

Instituto de Química y Fisicoquímica Biológicas
2015-2023

University of Buenos Aires
2014-2023

John Wiley & Sons (United States)
2020

Hudson Institute
2020

Instituto de Biotecnología y Biología Molecular
2016

University of Chieti-Pescara
1993-2011

Indonesian Institute of Sciences
2001

Virginia Commonwealth University Medical Center
1989

Abstract Objectives To investigate the molecular interaction between β-cyclodextrin (βCD) or hydroxypropyl-β-cyclodextrin (HPβCD) and riboflavin (RF), to test anticancer potential of these formulations. Methods The physicochemical characterization association RF CDs was performed by UV-vis absorption, fluorescence, differential scanning calorimetry NMR techniques. Molecular dynamics simulation used shed light on mechanism CDs. Additionally, in-vitro cell culture tests were evaluate...

10.1111/j.2042-7158.2012.01492.x article EN Journal of Pharmacy and Pharmacology 2012-03-16

The complete amino acid sequence of cytosolic serine hydroxymethyltransferase from rabbit liver was determined. determined analysis peptides isolated tryptic and cyanogen bromide cleavages the enzyme. Special procedures were used to isolate C-terminal blocked N-terminal peptides. Each four identical subunits enzyme consists 483 residues. could be easily aligned with Escherichia coli hydroxymethyltransferase. primary structural homology between E. enzymes is about 42%. importance predicted...

10.1016/s0021-9258(18)45600-1 article EN cc-by Journal of Biological Chemistry 1987-04-01

In this work; we investigated the differential interaction of amphiphilic antimicrobial peptides with 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine (POPC) lipid structures by means extensive molecular dynamics simulations. By using a coarse-grained (CG) model within MARTINI force field; simulated peptide-lipid system from three different initial configurations: (a) in water presence pre-equilibrated bilayer; (b) inside hydrophobic core membrane; and (c) random configurations that allow...

10.3390/molecules22101775 article EN cc-by Molecules 2017-10-20

The complete amino acid sequence of mitochondrial serine hydroxymethyltransferase from rabbit liver was determined. obtained analysis peptides isolated chymotryptic, cyanogen bromide, and limited cleavages the protein. enzyme consists four identical subunits, each 475 residues, i.e. 8 residues shorter than subunit corresponding cytosolic isoenzyme. sequences two proteins are easily aligned, provided a gap 5 near terminus 3 carboxyl included in sequence. overall degree identity between...

10.1016/s0021-9258(18)81821-x article EN cc-by Journal of Biological Chemistry 1989-05-01

Stevia species (Asteraceae) have been a rich source of terpenoid compounds, mainly sesquiterpene lactones, several which show antiprotozoal activity. In the search for new trypanocidal S. satureiifolia var. and alpina were studied. Two santhemoidin C 2-oxo-8-deoxyligustrin, respectively, isolated. These compounds assessed in vitro against Trypanosoma cruzi stages, showing IC50 values 11.80 4.98 on epimastigotes, 56.08 26.19 trypomastigotes 4.88 20.20 µM amastigotes, respectively....

10.3390/pharmaceutics15020647 article EN cc-by Pharmaceutics 2023-02-15

Alpha hemolysin of Escherichia coli (HlyA) is a pore-forming protein, which prototype the "Repeat in Toxins" (RTX) family. It was demonstrated that HlyA–cholesterol interaction facilitates insertion toxin into membranes. Putative cholesterol-binding sites, called cholesterol recognition/amino acid consensus (CRAC), and CARC (analogous to CRAC but with opposite orientation) were identified HlyA sequence. In this context, two peptides synthesized, one derived from site domain (residues...

10.1021/acs.biochem.3c00164 article EN Biochemistry 2023-05-24

Abstract Molecular dynamics simulations have been performed to investigate the interactions between nicotinamide (NA) and picolinamide (PA) with Langmuir monolayers of zwitterionic lipids: dimyristoylphosphatidylcholine (DMPC) dimyristoylphosphatidylethanolamine (DMPE). Our results for DMPC show that both NA PA molecules are essentially found at lipid/water interface present orientational disorder molecules. In case DMPE monolayers, pyridine nitrogen seems be located deeper inside monolayer...

10.1002/qua.24124 article EN International Journal of Quantum Chemistry 2012-05-24

Bovine serum amine oxidase is inhibited by benzylhydrazine (BHy), but recovers full activity after a few hours incubation [Hucko-Haas & Reed (1970) Biochem. Biophys. Res. Commun. 38, 396-400]. The first phase of the process, requiring about 15 min, was found to consist mechanism-based hydrazine-transfer reaction leading formation hydrazine-bound enzyme, benzaldehyde and H2O2. At variance with enzymic O2 preceded release. Two intermediates could be characterized optical spectroscopy were...

10.1042/bj2600019 article EN Biochemical Journal 1989-05-15

Abstract Iodoacetate reacts rapidly with one sulfhydryl group/subunit on aposerine transhydroxymethylase. The carboxymethylated apoenzyme does not recombine pyridoxal 5'-phosphate. Under conditions used in the studies, holoenzyme react to an appreciable extent iodoacetate. reaction of iodoacetate shows pseudo-first order kinetics a half-life about 3 min at 0 degrees C and pH 7.0. A pattern saturation was found when increasing concentrations were used. half-maximum rate inactivation occurred...

10.1016/s0021-9258(19)85839-8 article EN cc-by Journal of Biological Chemistry 1980-04-01
Coming Soon ...