TY  - GEN
A1  - Peter, Martin G.
A1  - Boldt, Peter C.
A1  - Niederstein, Yvonne
A1  - Peter-Katalinić, Jasna
T1  - Synthesen von Galactose-Cluster-haltigen Steroid-Derivaten
N2  - The synthesis of galactose clusters that are linked to a steroid moiety by a peptide-like spacer unit is described. The galactose cluster is obtained by Koenigs-Knorr glycosylation of TRIS-Gly-Fmoc (2b) under Helferich conditions. Peptide and ester bonds are formed after activation of carboxylic acids as diphenylthiophene dioxide (TDO) esters. 6a is synthesized in a convergent way by coupling of (Ac4Gal)3-TRIS-Gly (3e) with cholesteryl TDO succinate (5b). Coupling of (Ac4Gal)3-TRIS-Gly hydrogen succinate (3f) with Gly-O-Chol (5d) by means of EEDQ yields 6d. Reaction of (Ac4Gal)3-TRIS-Gly-SUCC-O-TDO (3g) with 25-hydroxycholesterol leads in a linear sequence to the oxysterol derivative 6f. Selective cleavage of the acetyl groups from galactose units yields the known compound 6b and the new derivatives 6e and 6g.
T3  - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - paper 042 
KW  - Glycoconjugates
KW  - Galactosides
KW  - Steroid esters
KW  - Amphiphiles
KW  - Glycopeptides
Y1  - 1990
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus-16783
ER  - 
TY  - GEN
A1  - Peter, Martin G.
A1  - Andersen, Svend Olav
A1  - Hartmann, Rudolf
A1  - Miessner, Merle
A1  - Roepstorff, Peter
T1  - Catecholamine-protein conjugates : isolation of 4-phenylphenoxazin-2-ones from oxidative coupling of N-acetyldopamine with alipathic amino acids
N2  - 4-Phenylphenoxazinones were isolated after biomimetic oxidation, using diphenoloxidases of insect cuticle, mushroom tyrosinase, or after autoxidation of N-acetyldopamine (Image ) in the presence of β-alanine, β-alanine methyl ester or N-acetyl-L-lysine. They are formed presumably by addition of 2-aminoalkyl-5-alkylphenols to the o-quinone of biphenyltetrol which, in turn, arises from oxidative coupling of. The structures of present the first examples for the assembly of reasonably stable intermediates in the rather complex process of chemical modifications of aliphatic amino acid residues by o-quinones.
T3  - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - paper 062 
Y1  - 1992
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus-17571
ER  - 
TY  - GEN
A1  - Peter, Martin G.
A1  - Stupp, Hans-Peter
A1  - Lentes, Klaus-Ulrich
T1  - Umkehr der Enantioselektivität bei der enzymatischen Hydrolyse von Juvenilhormon als Ergebnis einer Proteinfraktionierung
N2  - Aus dem Inhalt: Die Juvenilhormone 1a-c werden im Blut von Insekten enzymatisch zu den biologisch inaktiven Sluren hydrolysiert. Bei der Hydrolyse von racemischem 1c im Blut der Wanderheuschrecke Locusta migratoria wird ein Umsatz von 40-60% erreicht. Das unumgesetzte Edukt enthällt einen Überschuß an natürlich konfiguriertem (10R)-1c (e.e. 47.2%). Wir konnten zeigen, daß das in der Hämolymphe vorhandene Hormon-Bindungsprotein bevorzugt mit (10R)- 1c assoziiert.
T3  - Zweitveröffentlichungen der Universität Potsdam : Mathematisch-Naturwissenschaftliche Reihe - paper 052 
Y1  - 1983
U6  - http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:kobv:517-opus-17001
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  -