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  - 
TY  - JOUR
A1  - Germer, Antje
A1  - Peter, Martin G.
A1  - Kleinpeter, Erich
T1  - Solution-state conformational study of the hevamine inhibitor allosamidin and six potential inhibitor analogues by NMR spectroscopy and molecular modeling
N2  - 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.
Y1  - 2002
ER  - 
TY  - JOUR
A1  - Haebel, Sophie
A1  - Bahrke, Sven
A1  - Peter, Martin G.
T1  - Quantitative sequencing of complex mixtures of heterochitooligosaccharides by vMALDI-linear ion trap mass spectrometry
N2  - 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)].
Y1  - 2007
UR  - http://pubs.acs.org/loi/ancham
U6  - https://doi.org/10.1021/Ac062254u
SN  - 0003-2700
ER  - 
TY  - JOUR
A1  - Haebel, Sophie
A1  - Peter-Katalinic, Jasna
A1  - Peter, Martin G.
T1  - Mass spectrometry of chitooligosaccharides
Y1  - 1997
SN  - 88-86889- 01-1
ER  - 
TY  - JOUR
A1  - Houston, Douglas R.
A1  - Shiomi, Kazuro
A1  - Arai, Noriko
A1  - Omura, Satoshi
A1  - Peter, Martin G.
A1  - Turberg, Andreas
A1  - Synstad, Bjoenar
A1  - Eijsink, Vincent G. H.
A1  - Van Aalten, Daan M. F.
T1  - High-resolution structures of a chitinase complexed with natural product cyclopentapeptide inhibitors : mimicry of carbohydrate substrate
N2  - 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.
Y1  - 2002
ER  - 
TY  - JOUR
A1  - Issaree, Arisara
A1  - Vijayakrishnan, Balakumar
A1  - Abdelnur, Patricia V.
A1  - Corilo, Yuri E.
A1  - Riccio, Maria F.
A1  - Sanvido, Gustavo B.
A1  - Eberlin, Marcos N.
A1  - Peter, Martin G.
T1  - Mass spectrometry of aminoglucan oligosaccharides using electrospray ionization MS/MS and MS/MS/MS
Y1  - 2009
ER  - 
TY  - JOUR
A1  - Juma, Wanyama P.
A1  - Akala, Hoseah M.
A1  - Eyase, Fredrick L.
A1  - Muiva, Lois M.
A1  - Heydenreich, Matthias
A1  - Okalebo, Faith A.
A1  - Gitu, Peter M.
A1  - Peter, Martin G.
A1  - Walsh, Douglas S.
A1  - Imbuga, Mabel
A1  - Yenesew, Abiy
T1  - Terpurinflavone an antiplasmodial flavone from the stem of Tephrosia Purpurea
JF  - Phytochemistry letters
N2  - 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.
KW  - Tephrosia purpurea
KW  - Leguminosae
KW  - Stem
KW  - Flavone
KW  - Terpurinflavone
KW  - Antiplasmodial
Y1  - 2011
U6  - https://doi.org/10.1016/j.phytol.2011.02.010
SN  - 1874-3900
VL  - 4
IS  - 2
SP  - 176
EP  - 178
PB  - Elsevier
CY  - Amsterdam
ER  - 
TY  - JOUR
A1  - Kaatz, Helvi
A1  - Streffer, Katrin
A1  - Wollenberger, Ursula
A1  - Peter, Martin G.
T1  - Inhibition of mushroom tyrosinase by kojic acid octanoates
Y1  - 1999
ER  - 
TY  - JOUR
A1  - Kamlage, Stefan
A1  - Sefkow, Michael
A1  - Peter, Martin G.
T1  - A short synthesis of biologically active lignan analogues
N2  - beta-Benzyl-gamma-butyrolactones were synthesized in four transition metal catalysed reactions from butynediol, and alkylated to afford new, biologically active lignan analogues.
Y1  - 2001
ER  - 
TY  - JOUR
A1  - Kamlage, Stefan
A1  - Sefkow, Michael
A1  - Peter, Martin G.
T1  - Cross coupling of benzylic bromides and vinyl stannanes
Y1  - 1999
ER  - 
TY  - JOUR
A1  - Kamlage, Stefan
A1  - Sefkow, Michael
A1  - Zimmermann, Nicole
A1  - Peter, Martin G.
T1  - Concise synthesis of (+)-beta-benzyl gamma-butyrolactones from butynediol
Y1  - 2002
ER  - 
TY  - GEN
A1  - Kort, C. A. D. de
A1  - Peter, Martin G.
A1  - Koopmanschap, A. B.
T1  - Binding and degradation of juvenile hormone III by haemolymph proteins of the Colorado potato beetle: a re-examination
N2  - 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.
T3  - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - paper 068 
KW  - Juvenile hormone
KW  - Leptinotarsa decemlineata
KW  - JH-III-specific carrier protein
KW  - enantioselectivity
Y1  - 1983
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus-16777
ER  - 
TY  - JOUR
A1  - Krösche, Ch.
A1  - Peter, Martin G.
T1  - Detection of melanochromes by MALDI-TOF mass spectrometry
Y1  - 1996
ER  - 
TY  - JOUR
A1  - Krösche, Christian
A1  - Crescenzi, Orlando
A1  - Hoffbauer, Wilfried
A1  - Jansen, Martin
A1  - Napolitano, Alessandra
A1  - Prota, Guiseppe
A1  - Peter, Martin G.
T1  - 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
Y1  - 1994
ER  - 
TY  - JOUR
A1  - Letzel, Matthias C.
A1  - Peter-Katalinic, Jasna
A1  - Peter, Martin G.
T1  - Mass spectrometry of chitin and chitosan oligosaccharides
Y1  - 2001
ER  - 
TY  - JOUR
A1  - Letzel, Matthias C.
A1  - Synstad, Bjoenar
A1  - Eijsink, Vincent G. H.
A1  - Peter-Katalinic, Jasna
A1  - Peter, Martin G.
T1  - Libraries of chito-oligosaccharides of mixed acetylation patterns and their interactions with chitinases
Y1  - 1999
SN  - 3-9806494-5-8
ER  - 
TY  - JOUR
A1  - Ley, J. P.
A1  - Peter, Martin G.
T1  - Synthesis of L-histidine and (-)-spinacine chitooligosyl amides
Y1  - 1996
ER  - 
TY  - JOUR
A1  - Ley, J. P.
A1  - Peter, Martin G.
T1  - Synthesis of N-(2-Acetamido-2-deoxy-ß-D-glucopyranosyl)- and of N-(N,N-Diacetylchitobiosyl)-amide of lhistidine
Y1  - 1994
SN  - 0039-7881
ER  - 
TY  - JOUR
A1  - Ley, J. P.
A1  - Schweikart, F.
A1  - Peter, Martin G.
T1  - Chitinase inhibitors
Y1  - 1997
ER  - 
TY  - JOUR
A1  - Londershausen, M.
A1  - Turberg, Andreas
A1  - Bieseler, Barbara
A1  - Lennarz, M.
A1  - Peter, Martin G.
T1  - Characterization and Inhibitor Studies of Chitinases from Parasitic Blowfly (Lucilia cuprina), Tick (Boophilus micoplus), Intestinale Nematode (Haemonchus contortus), and a Bean (Phaseolus vulgaris)
Y1  - 1996
ER  -