TY  - JOUR
A1  - Norledge, Brian V.
A1  - Lambeir, Anne M.
A1  - Abagyan, Ruben
A1  - Rottmann, Antje
A1  - Fernendez, Anna M.
A1  - Filimonov, Vladimir V.
A1  - Peter, Martin G.
A1  - Wierenga, Rik K.
T1  - Modeling, mutagenesis, and structural studies on the fully conserved phoshate-binding loop (Loop 8) of triosephosphate isomerase : toward a new substrate specificity
Y1  - 2001
UR  - http://www3.interscience.wiley.com/journal/36176/toc
SN  - 0887-2585
ER  - 
TY  - JOUR
A1  - Rottmann, Antje
A1  - Synstad, Bjoenar
A1  - Thiele, G.
A1  - Schanzenbach, Dirk
A1  - Eijsink, Vincent G. H.
A1  - Peter, Martin G.
T1  - Approaches towards the design of new chitinase inhibitors
Y1  - 1999
SN  - 3-9806494-5-8
ER  - 
TY  - JOUR
A1  - Rottmann, Antje
A1  - Synstad, Bjoenar
A1  - Eijsink, Vincent G. H.
A1  - Peter, Martin G.
T1  - Synthesis of N-acetylglucosaminyl and diacetylchitobiosyl amides of heterocyclic carboxylic acids as potential chitinase inhibitors
Y1  - 1999
ER  - 
TY  - JOUR
A1  - Thiele, Gabriela
A1  - Rottmann, Antje
A1  - Germer, Antje
A1  - Kleinpeter, Erich
A1  - Spindler, Klaus-Dieter
A1  - Synstad, Bjoenar
A1  - Eijsink, Vincent G. H.
A1  - Peter, Martin G.
T1  - Synthesis and conformational analysis of pseudosugar analogues of chitotriose
N2  - In this article, the synthesis of analogs of N,N',N''-triacetylchitotriose in which the central sugar residue was replaced by a succinic acid is presented. Mol. modeling calcns. revealed that the pseudotrisaccharides exist in low energy extended conformations which show similar space filling as N,N',N''-triacetylchitotriose. Of the N,N',N''-triacetylchitotriose pseudosugar analogs tested as chitinase inhibitors, none showed any appreciable competition (numerical data not presented). The conformational anal. along with further synthetic efforts will hopefully lead to more efficient pseudosaccharides as chitinase inhibitors.
Y1  - 2002
ER  - 
TY  - JOUR
A1  - Germer, Antje
A1  - Mugge, Clemens
A1  - Peter, Martin G.
A1  - Rottmann, Antje
A1  - Kleinpeter, Erich
T1  - Solution- and bound-state conformational study of N,N',N''-triacetyl chitotriose and other analogous potential inhibitors of hevamine: Application of trNOESY and STD NMR spectroscopy
N2  - The soln.-state conformations of N,N',N''-triacetyl chitotriose (1) and other potential chitinase inhibitors 2-4 were studied using a combination of NMR spectroscopy (NOESY) and mol. mechanics calcns. Detn. solely of the global energy min. conformation was found to be insufficient for an agreement with the NMR results. An appropriate consistency between the NMR exptl. data and theor. calcns. was only reached by assessing the structures as population-weighted av. conformers based on Boltzmann distributions derived from the calcd. relative energies. Analogies, but also particular differences, between the synthetic compds. 2-4 and the naturally-occurring N,N',N''-triacetyl chitotriose were found. Furthermore, the conformation of compds. 1 and 2 when bound to hevamine was also studied using transferred NOESY expts. and the binding process was found to impart a level of conformational restriction on the ligands. The preferred conformation as detd. for 1 in the bound state to hevamine belonged to one of the conformational families found for the compd. when free in soln., although full characterization of the bound-state conformations was impeded due to severe signal overlap. Satn. transfer difference NMR expts. were also employed to analyze the binding epitopes of the bound compds. We thus detd. that it is mainly the acetyl amido groups of the trisaccharide and the heterocyclic moiety which are in close contact with hevamine.
Y1  - 2003
ER  -