@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{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{HaebelBahrkePeter2007,
  author    = {Haebel, Sophie and Bahrke, Sven and Peter, Martin G.},
  title     = {Quantitative sequencing of complex mixtures of heterochitooligosaccharides by vMALDI-linear ion trap mass spectrometry},
  issn      = {0003-2700},
  doi       = {10.1021/Ac062254u},
  year      = {2007},
  abstract  = {Heterochitooligosaccharides possess interesting biol. properties. Isobaric mixts. of such linear heterochitooligosaccharides can be obtained by chem. or enzymic degrdn. of chitosan. However, the sepn. of such mixts. is a challenging anal. problem which is so far unresolved. It is shown that these isobaric mixts. can be sequenced and quantified simultaneously using std. derivatization and multistage tandem mass spectrometric techniques. A linear ion trap mass spectrometer equipped with a vacuum matrix-assisted laser desorption ionization (vMALDI) source is used to perform MS2 as well as MS3 expts. [on SciFinder (R)].},
  language  = {en}
}
@article{HaebelPeterKatalinicPeter1997,
  author    = {Haebel, Sophie and Peter-Katalinic, Jasna and Peter, Martin G.},
  title     = {Mass spectrometry of chitooligosaccharides},
  isbn      = {88-86889- 01-1},
  year      = {1997},
  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{IssareeVijayakrishnanAbdelnuretal.2009,
  author    = {Issaree, Arisara and Vijayakrishnan, Balakumar and Abdelnur, Patricia V. and Corilo, Yuri E. and Riccio, Maria F. and Sanvido, Gustavo B. and Eberlin, Marcos N. and Peter, Martin G.},
  title     = {Mass spectrometry of aminoglucan oligosaccharides using electrospray ionization MS/MS and MS/MS/MS},
  year      = {2009},
  language  = {en}
}
@article{JumaAkalaEyaseetal.2011,
  author    = {Juma, Wanyama P. and Akala, Hoseah M. and Eyase, Fredrick L. and Muiva, Lois M. and Heydenreich, Matthias and Okalebo, Faith A. and Gitu, Peter M. and Peter, Martin G. and Walsh, Douglas S. and Imbuga, Mabel and Yenesew, Abiy},
  title     = {Terpurinflavone an antiplasmodial flavone from the stem of Tephrosia Purpurea},
  series = {Phytochemistry letters},
  volume    = {4},
  journal   = {Phytochemistry letters},
  number    = {2},
  publisher = {Elsevier},
  address   = {Amsterdam},
  issn      = {1874-3900},
  doi       = {10.1016/j.phytol.2011.02.010},
  pages     = {176 -- 178},
  year      = {2011},
  abstract  = {The stem extract of Tephrosia purpurea showed antiplasmodial activity against the D6 (chloroquine-sensitive) and W2 (chloroquine-resistant) strains of Plasmodium falciparum with IC(50) values of 10.47 +/- 2.22 mu g/ml and 12.06 +/- 2.54 mu g/ml, respectively. A new prenylated flavone, named terpurinflavone, along with the known compounds lanceolatin A, (-)-semiglabrin and lanceolatin B have been isolated from this extract. The new compound, terpurinflavone, showed the highest antiplasmodial activity with IC(50) values of 3.12 +/- 0.28 mu M (D6) and 6.26 +/- 2.66 mu M (W2). The structures were determined on the basis of spectroscopic evidence.},
  language  = {en}
}
@article{KaatzStrefferWollenbergeretal.1999,
  author    = {Kaatz, Helvi and Streffer, Katrin and Wollenberger, Ursula and Peter, Martin G.},
  title     = {Inhibition of mushroom tyrosinase by kojic acid octanoates},
  year      = {1999},
  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}
}
@article{KamlageSefkowPeter1999,
  author    = {Kamlage, Stefan and Sefkow, Michael and Peter, Martin G.},
  title     = {Cross coupling of benzylic bromides and vinyl stannanes},
  year      = {1999},
  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}
}
@misc{KortPeterKoopmanschap1983,
  author    = {Kort, C. A. D. de and Peter, Martin G. and Koopmanschap, A. B.},
  title     = {Binding and degradation of juvenile hormone III by haemolymph proteins of the Colorado potato beetle: a re-examination},
  url       = {http://nbn-resolving.de/urn:nbn:de:kobv:517-opus-16777},
  year      = {1983},
  abstract  = {The haemolymph of the adult Colorado potato beetle, Lepinotarsa decemlineata Say, contains a high molecular weight (MW > 200,000) JH-III specific binding protein. The Kd value of the protein for racemic JH-III is 1.3 ± 0.2 × 10-7 M. It has a lower affinity for racemic JH-I and it does not bind JH-III-diol or JH-III-acid. The binding protein does discriminate between the enantiomers of synthetic, racemic JH-III as was determined by stereochemical anaysis of the bound and the free JH-III. Incubation of racemic JH-III with crude haemolymph results in preferential formation of (10S)-JH-III-acid, the unnatural configuration. The JH-esterase present in L. decemlineata haemolymph is not enantioselective. It is concluded that the most important function of the binding protein is that of a specific carrier, protecting the natural hormone against degradation by esterases. The carrier does not protect JH-I as efficiently as the lower homologue.},
  language  = {en}
}
@article{KroeschePeter1996,
  author    = {Kr{\"o}sche, Ch. and Peter, Martin G.},
  title     = {Detection of melanochromes by MALDI-TOF mass spectrometry},
  year      = {1996},
  language  = {en}
}
@article{KroescheCrescenziHoffbaueretal.1994,
  author    = {Kr{\"o}sche, Christian and Crescenzi, Orlando and Hoffbauer, Wilfried and Jansen, Martin and Napolitano, Alessandra and Prota, Guiseppe and Peter, Martin G.},
  title     = {Synthesis of dopamines labelled with 13C in the alpha- or beta-side chain positions, and their application for structure studies on melanins by solid state NMR spectroscopy},
  year      = {1994},
  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{LetzelSynstadEijsinketal.1999,
  author    = {Letzel, Matthias C. and Synstad, Bjoenar and Eijsink, Vincent G. H. and Peter-Katalinic, Jasna and Peter, Martin G.},
  title     = {Libraries of chito-oligosaccharides of mixed acetylation patterns and their interactions with chitinases},
  isbn      = {3-9806494-5-8},
  year      = {1999},
  language  = {en}
}
@article{LeyPeter1996,
  author    = {Ley, J. P. and Peter, Martin G.},
  title     = {Synthesis of L-histidine and (-)-spinacine chitooligosyl amides},
  year      = {1996},
  language  = {en}
}
@article{LeyPeter1994,
  author    = {Ley, J. P. and Peter, Martin G.},
  title     = {Synthesis of N-(2-Acetamido-2-deoxy-ß-D-glucopyranosyl)- and of N-(N,N-Diacetylchitobiosyl)-amide of lhistidine},
  issn      = {0039-7881},
  year      = {1994},
  language  = {en}
}
@article{LeySchweikartPeter1997,
  author    = {Ley, J. P. and Schweikart, F. and Peter, Martin G.},
  title     = {Chitinase inhibitors},
  year      = {1997},
  language  = {en}
}
@article{LondershausenTurbergBieseleretal.1996,
  author    = {Londershausen, M. and Turberg, Andreas and Bieseler, Barbara and Lennarz, M. and Peter, Martin G.},
  title     = {Characterization and Inhibitor Studies of Chitinases from Parasitic Blowfly (Lucilia cuprina), Tick (Boophilus micoplus), Intestinale Nematode (Haemonchus contortus), and a Bean (Phaseolus vulgaris)},
  year      = {1996},
  language  = {en}
}