Maurizio Marta

Warsaw University of Life Sciences

Author Statistics

Papers

Citation

H-Index

i-10 index

Research Trends

Author Order

Document Type

Co-Authors

M. Pomponi

Università Cattolica del Sacro Cuore

Massimo Pomponi

Università Cattolica del Sacro Cuore

F. GATTA

Istituto Superiore di Sanità

Maria Patamia

National Research Council

Franco Delle Monachè

Universidade do Vale do Itajaí

M. Brufani

Universidade da Coruña

G.B. Marini-Bettòlo

Pontifical Academy of Sciences

Alessandro Lupi

Fondazione Audiologica Varese

Flaminia Pavone

Institute of Cell Biology and Neurobiology

Silvia Sacchi

University of Insubria

Cooperative Institutions

Università Cattolica del Sacro Cuore

Sapienza University of Rome

Istituti di Ricovero e Cura a Carattere Scientifico

Istituto di Chimica Biomolecolare

Policlinico San Matteo Fondazione

Istituto Superiore di Sanità

University of Milan

Agostino Gemelli University Polyclinic

Institute of Chemistry of Molecular Recognition

Universidad de La Laguna

Author Statistics

Papers

Citation

H-Index

i-10 index

Research Field

ChemInform Abstract: Physostigmines and Tetrahydroaminoacridine Analogues as Alternative Drugs for the Treatment of Alzheimer′s Disease.

ChemInform (1993)

M. Pomponi Bruno Giardina F. GATTA Maurizio Marta

Abstract ChemInform is a weekly Abstracting Service, delivering concise information at a glance that was extracted from about 100 leading journals. To access a ChemInform Abstract of an article which was published elsewhere, please select a “Full Text” option. The original article is trackable via the “References” option.

10.1002/chin.199308273

Cite

Citations (0)

Inhibition of Ache: Structure-Activity Relationship Among Conformational Transition of Trp84 and Bimolecular Rate Constant

Journal of enzyme inhibition (2000)

Claudia Bertonati Maurizio Marta Maria Patamia Annalisa Colella M. Pomponi

AbstractIn this study the authors attempt to correlate kinetic constants for carbamylation of AChE, by a series of carbamate inhibitors, with the conformational positioning of Trp84 in transition state complexes of the same carbamates with Torpedo AChE, as obtained by computerized molecular modelling. They present evidence for changes in the distance of the carbamates from the center of the indole ring which can be correlated with the bimolecular rate constants for inhibition. As a result the greater the distance from Trp84, the smaller the bimolecular inhibition constant value, k1 (= k2/Ka), becomes. In conclusion, the value of the biinolecular rate constant for selected AChE inhibitors (structural changes that have been hypothesised or natural alkaloids of unknown activity) which possess similar size and rigidity, can be obtained. Under these conditions energy minimization alone seems to be sufficient even to accurately predict protein-substrate interactions that actually occur. Modelling studies also suggest that conformational re-orientation of Trp84 in the transition state could produce an overall movement of the Cys67-Cys94 loop.Key Words: : Acetylcholinesterase catalysisCholinesterase inhibitionBimolecular rate constantsConformationsAlzheimer's disease

Carbamate

Rigidity (electromagnetism)

10.3109/14756360009040709

Cite

Citations (1)

New analogs of physostigmine: Alternative drugs for Alzheimer's disease?

Life Sciences (1988)

Maurizio Marta Claudio Castellano A. Oliverio Flaminia Pavone P.G. Pagella

Physostigmine

10.1016/s0024-3205(88)80010-9

Cite

Citations (40)

Studies on a new series of THA analogues: Effects of the aromatic residues that line the gorge of AChE

FEBS Letters (1997)

Massimo Pomponi Maurizio Marta Annalisa Colella Silvia Sacchi Maria Patamia

A series of N ‐monoalkylsubstituted 1,2,3,4‐tetrahydro‐9‐aminoacridines have been prepared after modelling simulation of the AChE–inhibitor complex. Molecular modelling has predicted a number of hydrophobic residues to be involved in the catalytic mechanism of this interaction between the binding sites of AChE and this series of aminoacridines. In these compounds the acridine moiety becomes sandwiched between the rings of PHE330 and TRP84. In particular, the alkyl chain shows the important role of aromatic groups as binding sites. Their in vitro inhibitory properties (enzyme from Electrophorus electricus ) confirm the aromatic groups as a general and significant characteristic of the mechanism of AChE inhibition.

Electrophorus

Acridine

Moiety

10.1016/s0014-5793(97)00492-4

Cite

Citations (7)

Synthesis of phenothiazine derivatives as potential inhibitors of phospholipase C.

PubMed (1992)

M. Brufani M C Cesta Luigi Filocamo Sperandina Lappa Maurizio Marta

Amide

Carboxamide

Tertiary amine

Source

Cite

Citations (1)

A long-lasting cholinesterase inhibitor affecting neural and behavioral processes

Pharmacology Biochemistry and Behavior (1987)

M. Brufani Claudio Castellano Maurizio Marta A. Oliverio P.G. Pagella

Cholinesterase

Physostigmine

Scopolamine

Tacrine

Acetylcholinesterase inhibitor

Rivastigmine

Locomotor activity

10.1016/0091-3057(87)90176-6

Cite

Citations (70)

Anticholinesterase activity of a new carbamate, heptylphysostigmine, in view of its use in patients with Alzheimer-type dementia

European Journal of Biochemistry (1986)

Mario Brufani Maurizio Marta Massimo Pomponi

The anticholinesterase activity of a new carbamate, heptylphysostigmine, was studied in vitro. This compound is a competitive inhibitor of acetylcholinesterase (or true cholinesterase) having Ki= (1 ± 0.5) × 10−7 M. The inhibition was instantaneous at the onset and did not diminish with prolonged incubation of the drug and enzyme.

Cholinesterase

Carbamate

10.1111/j.1432-1033.1986.tb09646.x

Cite

Citations (78)

Physostigmine analogs anticholinesterases: effects of the lengthening of the N-carbamic chain of the inhibition kinetics

Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics (1992)

Maurizio Marta F. GATTA Massimo Pomponi

Physostigmine

Electronic effect

Cholinesterase

10.1016/0167-4838(92)90246-a

Cite

Citations (15)

Bovine Hemoglobin Cross-Linked through the β Chains

Journal of Biological Chemistry (1996)

Maurizio Marta Maria Patamia Alessandro Lupi Mirca Antenucci Mario Iorio

2-Nor-2-formylpyridoxal (NFPLP) has been synthesized and coupled to bovine Hb according to the procedure developed by Benesch and Benesch(1.Benesch R. Benesch R.E. Methods Enzymol. 1981; 76: 147-159Crossref PubMed Scopus (53) Google Scholar). The reaction of bovine Hb with NFPLP leads to a cross-linkage between the β subunits, which greatly stabilizes the low affinity T state of the molecule and simultaneously abolishes the tendency of the tetramer to dissociate into αβ dimers. The functional properties, examined from both the equilibrium and kinetic points of view, indicate that the chemical modification affects the O2 affinity, abolishes cooperativity, and induces a slight decrease of the Bohr effect. From modeling studies we are confronted with two different structural alternatives; the cross-link of β chains may be formed between lysine 82 of β2 and the N terminus of methionine 2 of β1 or between the two lysine 82 residues of both β2 chains. Digestion of modified β globin chains and isolation of the cross-linked peptide have showed that NFPLP cross-links Met-β2 and Lys-β82. This allowed discussion in some detail of the molecular basis of the Bohr effect of the modified bovine hemoglobin. On the whole, NFPLP-modified bovine Hb could be considered as a first step toward the synthesis of a potential blood substitute. 2-Nor-2-formylpyridoxal (NFPLP) has been synthesized and coupled to bovine Hb according to the procedure developed by Benesch and Benesch(1.Benesch R. Benesch R.E. Methods Enzymol. 1981; 76: 147-159Crossref PubMed Scopus (53) Google Scholar). The reaction of bovine Hb with NFPLP leads to a cross-linkage between the β subunits, which greatly stabilizes the low affinity T state of the molecule and simultaneously abolishes the tendency of the tetramer to dissociate into αβ dimers. The functional properties, examined from both the equilibrium and kinetic points of view, indicate that the chemical modification affects the O2 affinity, abolishes cooperativity, and induces a slight decrease of the Bohr effect. From modeling studies we are confronted with two different structural alternatives; the cross-link of β chains may be formed between lysine 82 of β2 and the N terminus of methionine 2 of β1 or between the two lysine 82 residues of both β2 chains. Digestion of modified β globin chains and isolation of the cross-linked peptide have showed that NFPLP cross-links Met-β2 and Lys-β82. This allowed discussion in some detail of the molecular basis of the Bohr effect of the modified bovine hemoglobin. On the whole, NFPLP-modified bovine Hb could be considered as a first step toward the synthesis of a potential blood substitute.

Tetramer

Cooperativity

Bohr effect

10.1074/jbc.271.13.7473

Cite

Citations (16)

ChemInform Abstract: Synthesis of 1,2,3,4‐Tetrahydroacridine and 5,6,7,8‐Tetrahydroquinoline Derivatives as Potential Acetylcholinesterase Inhibitors.

ChemInform (1992)

F. GATTA Maria Rosaria Del Giudice M. Pomponi Maurizio Marta

10.1002/chin.199234174

Cite

Citations (1)