@phdthesis{DereseYenesewMidiwoetal.2003,
  author    = {Derese, Solomon and Yenesew, Abiy and Midiwo, Jacob O. and Heydenreich, Matthias and Peter, Martin G.},
  title     = {A new isoflavone from stem bark of Millettia dura},
  issn      = {1011-3924},
  year      = {2003},
  language  = {en}
}
@article{GermerMuggePeteretal.2003,
  author    = {Germer, Antje and Mugge, Clemens and Peter, Martin G. and Rottmann, Antje and Kleinpeter, Erich},
  title     = {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},
  year      = {2003},
  abstract  = {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.},
  language  = {en}
}
@article{KamlageSefkowZimmermannetal.2002,
  author    = {Kamlage, Stefan and Sefkow, Michael and Zimmermann, Nicole and Peter, Martin G.},
  title     = {Concise synthesis of (+)-beta-benzyl gamma-butyrolactones from butynediol},
  year      = {2002},
  language  = {en}
}
@article{Peter2002,
  author    = {Peter, Martin G.},
  title     = {Chitin and Chitosan from Animal Sources},
  isbn      = {3-527-30227-1},
  year      = {2002},
  abstract  = {A review on the chem. and biochem. of chitin and the chem. and application of chitosan. The following topics were discussed: structure of chitin and chitosan; occurrence and physiol. functions of chitin; detection of chitin in animals and anal. of chitin and chitosan; biosynthesis and biodegrdn. of chitin in animals; prodn. of chitin and chitosan; properties of chitin and chitosan; and applications of chitin and chitosan.},
  language  = {en}
}
@article{Peter2002,
  author    = {Peter, Martin G.},
  title     = {Chitin and Chitosan from Fungi},
  isbn      = {3-527-30227-1},
  year      = {2002},
  language  = {en}
}
@article{YenesewMidiwoGuchuetal.2002,
  author    = {Yenesew, Abiy and Midiwo, Jacob O. and Guchu, S. M. and Heydenreich, Matthias and Peter, Martin G.},
  title     = {Three iosoflav-3-enes and a 2-arylbenzofuran from the root bark of Erythrina burttii},
  year      = {2002},
  abstract  = {From the root bark of Erythrina burttii three new isoflav-3-enes, 7,4'-dihydroxy-2'-methoxy-6- (1'',1''-dimethylallyl)isoflav-3-ene (trivial name, burttinol-A), 4'-hydroxy-2'- methoxy-(2'',2''-dimethylpyrano[5'',6'':8,7]isoflav-3-ene (trivial name, burttinol-B), 7,4'-dihydroxy-2'-methoxy-8-(3'',3''-dimethylallyl)isoflav-3-ene (trivial name, burttinol-C), and a new 2-arylbenzofuran, 6,4'-dihydroxy-2'-methoxy-5- (1'',1''-dimethylallyl)-2-arylbenzofuran (trivial name, burttinol-D) were isolated. In addition, the known compounds, abyssinone V-4'-methyl ether, bidwillol A, calopocarpin, erybraedin A, erythrabyssin II, isobavachalcone, phaseollidin and phaseollin were identified. The structures were determined on the basis of spectroscopic evidence.},
  language  = {en}
}
@article{BahrkeEinarssonGislasonetal.2002,
  author    = {Bahrke, Sven and Einarsson, Jon M. and Gislason, Johannes and Haebel, Sophie and Letzel, Matthias C. and Peter-Katalinic, Jasna and Peter, Martin G.},
  title     = {Sequence analysis of chitooligosaccharides by matrix-assisted laser desorption ionization postsource decay mass spectrometry},
  year      = {2002},
  abstract  = {Oligosaccharides composed of 2-acetamido-2-deoxy-D-glucopyranose (GlcNAc) and/or 2-amino-2-deoxy-D- glucopyranose (GlcN) were prepd. by chem. degrdn. of chitin or chitosan and sepd. by gel permeation chromatog. Oligosaccharides obtained after enzymic hydrolysis of chitosan [FA 0.19] with a fungal chitinase were derivatized by reductive amination with 2-aminoacridone and sequenced by matrix-assisted laser desorption ionization time-of-flight postsource decay (PSD) mass spectrometry (MS). The sequence of a trimer, D1A2, was established as D-A-A. The compn. of a hexamer D3A3 was .apprx.65\% D-A-D-D-A-A and 35\% D-D-A-D-A-A. The PSD MS of a nonamer D5A4-amac revealed four isobaric species D-X-Y-D-X-Y-D-A-A, where A is GlcNAc, D is GlcN, and X and Y (X ¹ Y) are mutually either D or A. This structure motif was also obsd. in a dodecamer D7A5 which was composed of eight isobaric sequences of the general formula (D-X-Y)3- D-A-A.},
  language  = {en}
}
@article{HoustonShiomiAraietal.2002,
  author    = {Houston, Douglas R. and Shiomi, Kazuro and Arai, Noriko and Omura, Satoshi and Peter, Martin G. and Turberg, Andreas and Synstad, Bjoenar and Eijsink, Vincent G. H. and Van Aalten, Daan M. F.},
  title     = {High-resolution structures of a chitinase complexed with natural product cyclopentapeptide inhibitors : mimicry of carbohydrate substrate},
  year      = {2002},
  abstract  = {Over the past years, family 18 chitinases have been validated as potential targets for the design of drugs against human pathogens that contain or interact with chitin during their normal life cycles. Thus far, only one potent chitinase inhibitor has been described in detail, the pseudotrisaccharide allosamidin. Recently, however, two potent natural-product cyclopentapeptide chitinase inhibitors, argifin and argadin, were reported. Here, we describe high- resoln. crystal structures that reveal the details of the interactions of these cyclopeptides with a family 18 chitinase. The structures are examples of complexes of a carbohydrate-processing enzyme with high-affinity peptide-based inhibitors and show in detail how the peptide backbone and side chains mimic the interactions of the enzyme with chitooligosaccharides. Together with enzymol. characterization, the structures explain why argadin shows an order of magnitude stronger inhibition than allosamidin, whereas argifin shows weaker inhibition. The peptides bind to the chitinase in remarkably different ways, which may explain the differences in inhibition consts. The two complexes provide a basis for structure-based design of potent chitinase inhibitors, accessible by std. peptide chem.},
  language  = {en}
}
@article{vanAaltenKomanderSynstadetal.2002,
  author    = {van Aalten, Daan M. F. and Komander, David and Synstad, Bjoenar and Gaseidnes, Sigrid and Peter, Martin G. and Eijsink, Vincent G. H.},
  title     = {Structural Insights into the catalytic mechanism of a family 18 exochitinase},
  year      = {2002},
  abstract  = {Chitinase B (ChiB) from Serratia marcescens is a family 18 exochitinase whose catalytic domain has a TIM-barrel fold with a tunnel-shaped active site. We have solved structures of three ChiB complexes that reveal details of substrate binding, substrateassisted catalysis, and product displacement. The structure of an inactive ChiB mutant (E144Q) complexed with a pentameric substrate (binding in subsites 22 to 13) shows closure of the ''roof'' of the active site tunnel. It also shows that the sugar in the 21 position is distorted to a boat conformation, thus providing structural evidence in support of a previously proposed catalytic mechanism. The structures of the active enzyme complexed to Allosamidin (an analogue of a proposed reaction intermediate) and of the active enzyme soaked with pentameric substrate show events after cleavage of the glycosidic bond. The latter structure shows reopening of the roof of the active site tunnel and enzyme-assisted product displacement in the 11 and 12 sites, allowing a water molecule to approach the reaction center. Catalysis is accompanied by correlated structural changes in the core of the TIM barrel that involve conserved polar residues whose functions were hitherto unknown. These changes simultaneously contribute to stabilization of the reaction intermediate and alternation of the pKa of the catalytic acid during the catalytic cycle.},
  language  = {en}
}
@article{ThieleRottmannGermeretal.2002,
  author    = {Thiele, Gabriela and Rottmann, Antje and Germer, Antje and Kleinpeter, Erich and Spindler, Klaus-Dieter and Synstad, Bjoenar and Eijsink, Vincent G. H. and Peter, Martin G.},
  title     = {Synthesis and conformational analysis of pseudosugar analogues of chitotriose},
  year      = {2002},
  abstract  = {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.},
  language  = {en}
}
@article{GermerPeterKleinpeter2002,
  author    = {Germer, Antje and Peter, Martin G. and Kleinpeter, Erich},
  title     = {Solution-state conformational study of the hevamine inhibitor allosamidin and six potential inhibitor analogues by NMR spectroscopy and molecular modeling},
  year      = {2002},
  abstract  = {The soln.-state conformations of the hevamine inhibitor allosamidin and six potential inhibitor analogs were studied by various NMR spectroscopic techniques and mol. modeling using force field calcns. Detn. solely of the global energy min. conformation was found to be insufficient for consensus with the NMR results, and agreement between the NMR exptl. data and the theor. calcns. was only reached by assessing the structures as population-weighted av. conformers on the basis of Boltzmann distributions derived from the calcd. relative energies. The conformations of the glycosidic linkages in the compds. were found to be similar when the sugar residues were the same, but differences were markedly evident otherwise and also for the various heterocyclic group linkages. The binding of the compds. to hevamine, which may also complex to chitinases in general, was assessed using HMQC, transfer-NOESY, and both 1-D and 2-D satn. transfer difference NMR expts. Under the conditions employed, only allosamidin was implicated to be bound to hevamine, and then only by HMQC with the dipolar coupling-based expts. failing to substantiate the formation of the complex. However, the results are consistent with the biochem. activities of the compds. whereby only allosamidin has been shown to act as a competitive inhibitor.},
  language  = {en}
}
@article{GermerKlodPeteretal.2002,
  author    = {Germer, Antje and Klod, Sabrina and Peter, Martin G. and Kleinpeter, Erich},
  title     = {NMR spectroscopic and theoretical study of the complexation of the inhibitor allosamidin in the binding pocket of the plant chitinase hevamine},
  year      = {2002},
  abstract  = {Based on NMR spectroscopic information about the allosamidin-hevamine complex, ab initio MO calcns. of the ring current effect of the arom. moieties of Trp255, Tyr183 and Tyr6 of hevamine were carried out to investigate the role of these amino acid residues in binding interactions with allosamidin in soln. In addn., the intermol. steric compression effect on the 13C chem. shifts of the allosamizoline carbon atoms and the hydrogen bonding to Glu127 was identified. It can be inferred that the binding forces are strongest in the allosamizoline moiety of allosamidin.},
  language  = {en}
}
@article{NorledgeLambeirAbagyanetal.2001,
  author    = {Norledge, Brian V. and Lambeir, Anne M. and Abagyan, Ruben and Rottmann, Antje and Fernendez, Anna M. and Filimonov, Vladimir V. and Peter, Martin G. and Wierenga, Rik K.},
  title     = {Modeling, mutagenesis, and structural studies on the fully conserved phoshate-binding loop (Loop 8) of triosephosphate isomerase : toward a new substrate specificity},
  issn      = {0887-2585},
  year      = {2001},
  language  = {en}
}
@article{MiessnerPeterVincent2001,
  author    = {Miessner, Merle and Peter, Martin G. and Vincent, Julian F. V.},
  title     = {Preparation of Insect-Cuticle-Like Biomimetic Materials},
  year      = {2001},
  abstract  = {A model system of tanning of a protein matrix within a fibrous structure, such as most commonly found in insect cuticle, was developed, using the cellulose of paper in place of chitin. The paper was impregnated with a tripeptide, DOPA-Gly-Gly, or a protein (BSA) plus catechol and treated with tyrosinase to oxidize the catechol. The resulting material was waterproof and had very high wet strength. If the material was wetted and dried repeatedly its water retention decreased by a factor of at least two.},
  language  = {en}
}
@article{Peter2001,
  author    = {Peter, Martin G.},
  title     = {Nat{\"u}rliche Klebstoffe : von Muscheln, Seepocken, Spinnen und anderem Klebe-Getier},
  isbn      = {3-519-16195-8},
  year      = {2001},
  language  = {de}
}
@article{ZalaStruszczykPeter2001,
  author    = {Zala, Eva and Struszczyk, Marcin Henryk and Peter, Martin G.},
  title     = {Effects of preparation methods for chitosan films on their properties},
  year      = {2001},
  language  = {en}
}
@article{Peter2001,
  author    = {Peter, Martin G.},
  title     = {Structures of Chitinases and the Design of Inhibitors},
  year      = {2001},
  language  = {en}
}
@article{LetzelPeterKatalinicPeter2001,
  author    = {Letzel, Matthias C. and Peter-Katalinic, Jasna and Peter, Martin G.},
  title     = {Mass spectrometry of chitin and chitosan oligosaccharides},
  year      = {2001},
  language  = {en}
}
@article{StruszczykLothPospiesznyetal.2001,
  author    = {Struszczyk, Marcin Henryk and Loth, Fritz and Pospieszny, Henryk and Peter, Martin G.},
  title     = {Biodegradation of films and paper sheets containing chitosan},
  year      = {2001},
  language  = {en}
}
@article{KamlageSefkowPeter2001,
  author    = {Kamlage, Stefan and Sefkow, Michael and Peter, Martin G.},
  title     = {A short synthesis of biologically active lignan analogues},
  year      = {2001},
  abstract  = {beta-Benzyl-gamma-butyrolactones were synthesized in four transition metal catalysed reactions from butynediol, and alkylated to afford new, biologically active lignan analogues.},
  language  = {en}
}