Colella A

References (2)

Title : The role of TRP84 in catalytic power and the specificity of AChE - Pomponi_1998_Biophys.Chem_72_239
Author(s) : Pomponi M , Sacchi S , Colella A , Patamia M , Marta M
Ref : Biophysical Chemistry , 72 :239 , 1998
Abstract : The structure-function relationship between the alkaloids physostigmine, physovenine and the three structurally related compounds were investigated by employing kinetic studies and molecular modeling. Crystallographic data from the X-ray conformation of the Torpedo californica acetylcholinesterase complex together with the transition state analog inhibitor m-(N,N,N,-Trimethylammonio) trifluoroacetophenone (TMTFA) was used as template onto which inhibitors were superimposed. Among the structural elements of the active site, TRP84 residue shows a versatile role. In fact, its aromatic electrons not only can be employed in pi-cation interactions, as is the case for ACh, but they can also provide a polarizable surface for van der Waals and London interactions.
ESTHER : Pomponi_1998_Biophys.Chem_72_239
PubMedSearch : Pomponi_1998_Biophys.Chem_72_239
PubMedID: 9691268

Title : Studies on a new series of THA analogues: effects of the aromatic residues that line the gorge of AChE - Pomponi_1997_FEBS.Lett_409_155
Author(s) : Pomponi M , Marta M , Colella A , Sacchi S , Patamia M , Gatta F , Capone F , Oliverio A , Pavone F
Ref : FEBS Letters , 409 :155 , 1997
Abstract : 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.
ESTHER : Pomponi_1997_FEBS.Lett_409_155
PubMedSearch : Pomponi_1997_FEBS.Lett_409_155
PubMedID: 9202137