Maurizio Remelli was born in Ferrara in 1959. He graduated in Chemistry with first class honors in 1984, with prof. Francesco Dondi, with a thesis in Analytical Chemistry on “Study of the peak shape in Gas chromatography”. During his thesis he had a research fellowship at the Laboratoire peak de Chimie Analytique Physique of Ecóle Polytecnique (Palaiseau, Paris), with prof. George Guiochon.
In 1990 he received the PhD graduation in Chemical Sciences at the University of Ferrara, with prof. Fernando Pulidori as supervisor. The PhD thesis was about “Thermodynamic stereoselectivity of ternary Cu(II) complexes with amino acids; applications to the chromatographic separation of enantiomeric mixtures”.
After a 6-month scholarship financed by CINECA consortium ad a two-year experience in a private industry (Himont), Maurizio Remelli was hired as a technician of the Chemical Institute of the University of Ferrara.
In 1995 he became Assistant Professor and in 2001 Associate Professor in Analytical Chemistry, at the Chemistry Department of Ferrara University (nowadays named Department of Chemical, Pharmaceutical and Agricultural Sciences), of which he was vice-director from 1/08/2006 to 03/09/2012. On 12/04/2017, Maurizio Remelli obtained the national habilitation for Full Professor in Analytical Chemistry.
Prof. Maurizio Remelli's scientific interest has been first devoted to chromatographic studies, concerning: a) stochastic theory of Chromatography and its possible applications to chromatographic-instrument characterization; b) planning, preparation and investigation of chiral stationary phases for HPTLC and HPLC, obtained through a dynamical procedure and based on a Ligand-Exchange mechanism.
However, his main scientific activity has been developed in the field of solution equilibria, with especial concern to thermodynamics of labile-complex formation between metal cations and biologically relevant ligands. Among them:
- natural and synthetic amino acids and oligopeptides;
- emerging contaminants like non-steroidal anti-inflammatory agents;
- fragments of the natural matricellular protein SPARC (a human protein with angiogenic properties);
- wild and synthetically modified fragments of the prion protein, which plays a key role in the onset, transmission and development of the human Creutzfeld-Jacob disease and in the Bovine Spongiform Encefalopathy;
- fragments of the protein encoded by the gene Park9 and of α-Synuclein, both playing a key role in Parkinson's disease;
- R-1 and R-3 fragments of tau protein, present in significant amounts in neurons and associated with several neurological disorders known as tauopathies, among which is Alzheimer's disease;
- model peptides derived Hpn, a nickel-binding protein secreted by Helicobacter Pylori;
- AGHLDDLPGALSAL: a hemoglobin fragment potentially competing with albumin to bind transition metal ions;
- hemopressin, a neuropeptide, derived from the degradation of the alpha(1)-chain of hemoglobin;
- fragments of a protein sequence of 199 amino acid residues (C4YJH2) considered a putative Zn(II) transporter in opportunistic yeast species Candida albicans;
- calcitermin, a well-conserved antimicrobial peptide from the fluid of the human airways, consisting of a sequence of 15 amino acid and derived from the C-terminal cleavage of calgranulin C;
- fragments of ZinT, a highly conserved periplasmic protein expressed by different bacterial species;
- poly-histidine peptides isolated from snake venoms and related derivatives;
- newly designed and synthesized branched peptides, obtained by mounting linear peptides on a cyclam-based scaffold, candidate as “synthetic enzymes”;
- mono-hydroxamic and amino-hydroxamic acids which can form, in the presence of copper(II) or nickel(II) ions, supramolecular structure called metallacrowns;
- chelating agents for the oral treatment of iron and aluminum overload diseases;
Many experimental techniques have been employed for such investigations: protonation and complex-formation constants are potentiometrically determined; formation enthalpies are measured by direct solution calorimetry; complex-formation model and species stoichiometry are carefully checked by means of UV-VIS absorption, CD, NMR and EPR spectroscopies and Mass Spectrometry. X-ray diffractometry was also employed, when possible, to compare complex structures in the solid and in the solution state. Molecular modelling computation has been often employed to support the structural hypotheses of solution complexes.
These studies have been performed in cooperation with several Italian and European research groups.
The publication record of prof. Maurizio Remelli consists of about a hundred of publications on international peer-reviewed journals, with a total of 2.688 citations (2.383 without self-citations) and a h-index of 30 (on 12-01-2021). In addition, he counts more than 150 congress presentations and one national patent.
(Last revision: march 5, 2021)
In 1990 he received the PhD graduation in Chemical Sciences at the University of Ferrara, with prof. Fernando Pulidori as supervisor. The PhD thesis was about “Thermodynamic stereoselectivity of ternary Cu(II) complexes with amino acids; applications to the chromatographic separation of enantiomeric mixtures”.
After a 6-month scholarship financed by CINECA consortium ad a two-year experience in a private industry (Himont), Maurizio Remelli was hired as a technician of the Chemical Institute of the University of Ferrara.
In 1995 he became Assistant Professor and in 2001 Associate Professor in Analytical Chemistry, at the Chemistry Department of Ferrara University (nowadays named Department of Chemical, Pharmaceutical and Agricultural Sciences), of which he was vice-director from 1/08/2006 to 03/09/2012. On 12/04/2017, Maurizio Remelli obtained the national habilitation for Full Professor in Analytical Chemistry.
Prof. Maurizio Remelli's scientific interest has been first devoted to chromatographic studies, concerning: a) stochastic theory of Chromatography and its possible applications to chromatographic-instrument characterization; b) planning, preparation and investigation of chiral stationary phases for HPTLC and HPLC, obtained through a dynamical procedure and based on a Ligand-Exchange mechanism.
However, his main scientific activity has been developed in the field of solution equilibria, with especial concern to thermodynamics of labile-complex formation between metal cations and biologically relevant ligands. Among them:
- natural and synthetic amino acids and oligopeptides;
- emerging contaminants like non-steroidal anti-inflammatory agents;
- fragments of the natural matricellular protein SPARC (a human protein with angiogenic properties);
- wild and synthetically modified fragments of the prion protein, which plays a key role in the onset, transmission and development of the human Creutzfeld-Jacob disease and in the Bovine Spongiform Encefalopathy;
- fragments of the protein encoded by the gene Park9 and of α-Synuclein, both playing a key role in Parkinson's disease;
- R-1 and R-3 fragments of tau protein, present in significant amounts in neurons and associated with several neurological disorders known as tauopathies, among which is Alzheimer's disease;
- model peptides derived Hpn, a nickel-binding protein secreted by Helicobacter Pylori;
- AGHLDDLPGALSAL: a hemoglobin fragment potentially competing with albumin to bind transition metal ions;
- hemopressin, a neuropeptide, derived from the degradation of the alpha(1)-chain of hemoglobin;
- fragments of a protein sequence of 199 amino acid residues (C4YJH2) considered a putative Zn(II) transporter in opportunistic yeast species Candida albicans;
- calcitermin, a well-conserved antimicrobial peptide from the fluid of the human airways, consisting of a sequence of 15 amino acid and derived from the C-terminal cleavage of calgranulin C;
- fragments of ZinT, a highly conserved periplasmic protein expressed by different bacterial species;
- poly-histidine peptides isolated from snake venoms and related derivatives;
- newly designed and synthesized branched peptides, obtained by mounting linear peptides on a cyclam-based scaffold, candidate as “synthetic enzymes”;
- mono-hydroxamic and amino-hydroxamic acids which can form, in the presence of copper(II) or nickel(II) ions, supramolecular structure called metallacrowns;
- chelating agents for the oral treatment of iron and aluminum overload diseases;
Many experimental techniques have been employed for such investigations: protonation and complex-formation constants are potentiometrically determined; formation enthalpies are measured by direct solution calorimetry; complex-formation model and species stoichiometry are carefully checked by means of UV-VIS absorption, CD, NMR and EPR spectroscopies and Mass Spectrometry. X-ray diffractometry was also employed, when possible, to compare complex structures in the solid and in the solution state. Molecular modelling computation has been often employed to support the structural hypotheses of solution complexes.
These studies have been performed in cooperation with several Italian and European research groups.
The publication record of prof. Maurizio Remelli consists of about a hundred of publications on international peer-reviewed journals, with a total of 2.688 citations (2.383 without self-citations) and a h-index of 30 (on 12-01-2021). In addition, he counts more than 150 congress presentations and one national patent.
(Last revision: march 5, 2021)
