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Die tert.-Butyloxycarbonyl-Gruppe (Boc) läßt sich mittels reiner Trifluoressigsäure nicht selektiv neben dem Benzyloxycarbonyl-Rest (Z) abspalten. Das gelingt auch nicht mit Lösungen von Trifluoressigsäure bzw. Chlorwasserstoff in organischen Lösungsmitteln. Kern-substituierte Z-Gruppen wie Z(pCl), Z(mCl) oder Z(pNO₂) sind zwar stabiler, werden aber von den obengenannten Reagenzien ebenfalls angegriffen bzw. sind nicht mehr acidolytisch abspaltbar. – Mit 70proz. wäßriger Trifluoressigsäure gelingt die Abspaltung von Boc neben Z dagegen fast selektiv; dabei werden aber Benzylester, besonders Glutaminsäure-γ-benzylester, teilweise hydrolysiert, während Methyl- sowie Äthylester nahezu beständig sind. Die Brauchbarkeit des Abspaltungsverfahrens wird anhand der schrittweise durchgeführten Synthese zweier Heptapeptid-Derivate gezeigt. – Ähnlich spezifisch gelingt die Abspaltung von Boc mit Bortrifluorid-ätherat in Eisessig; Benzylester sind gegenüber diesem Reagenz stabiler als gegen wäßrige Trifluoressigsäure. Das Bortrifluorid-Verfahren eignet sich besonders für die Abspaltung von Boc-Gruppen neben säurelabilen Thiol-Schutzgruppen (Tetrahydropyranyl- bzw. Trityl-Rest) sowie neben dem Cyclocystinyl-Rest. Die Leistungsfähigkeit der Methode wird durch die Synthese zweier Peptid-Derivate mit S-Trityl-Schutzgruppen belegt. Als Nebenreaktion ist die Acetylierung von aliphatischen Hydroxylgruppen möglich. Sie läßt sich vermeiden, wenn man die Spaltung in anderen Lösungsmitteln durchführt. Die als Modellverbindungen für Stabilitätsuntersuchungen verwendeten Nε-acylierten Lysin-Derivate werden mit dem Aminosäureanalysator quantitativ neben Lysin bestimmt.
Es wird die Synthese der Sequenz A 6–9 des Schafinsulins in der geschützten Form Boc-Cys-Cys-Ala-Gly-OBuᵗ (5) sowie das Verhalten dieses monomeren cyclischen Cystinpeptidderivates gegenüber den in der Peptidchemie gebräuchlichen Reagenzien Bortrifluorid/Eisessig, Triäthylamin und Hydrazinhydrat beschrieben.
Die Darstellung der N-[2-(p-Biphenylyl)isopropyloxycarbonyl]-Derivate (Bpoc-Derivate) des Cysteins unter Verwendung der Thiolschutzgruppen Tetrahydropyranyl (Thp) für 1, Diphenylmethyl (Dpm) für 2, Trityl (Trt) für 3 und S-tert.-Butyl (SBut) für 4 sowie die Synthese von aktivierten Estern der Bpoc-Derivate des Glycins (5), Isoleucins (6) und Prolins (7) werden beschrieben. An einem Beispiel wird die Möglichkeit aufgezeigt, die Bpoc-Gruppe über das Bpoc-Azid nachträglich in den Peptidverband einzuführen.
Die Synthese der Sequenzen A2—21 (13) und A1—21 (15) der Schafinsulin-A-Kette als monomere cyclische Dicystinpeptidderivate wird beschrieben. Die intrachenaren Cystinbrücken A6—7 und A 11 —20 vermitteln die Löslichkeit dieser Derivate in Dimethylformamid und ermöglichen erstmalig die Reindarstellung vollgeschützter Insulin-A-Kettenderivate. Die während der Synthese eingesetzten Schutzgruppen lassen sich mittels Trifluoressigsäure und 2-Mercaptoäthanol quantitativ entfernen.
Thermal synthesis of the optical pure pentapeptide derivative Z-(L)-Ala-(L)-Phe-Gly-(L)-Phe-Gly-OMe
(1980)
Synthese der Sequenz 71—86 des Humanproinsulins, III : Synthese über die Fragmente 71—78 und 79—86
(1979)
Zur Synthese der Hühnerinsulin-A-Kette, I : Darstellung der Fragmente A1–8, A9–15, A1–7 und A8–15
(1979)
Danho, Waleed ; Naithani, Vinod K. ; Sasaki, André N. ; Föhles, Joseph ; Berndt, Heinz ; Büllesbach, Erika E. ; Zahn, H.
Kalbe, Jochen ; Kuropka, Rolf ; Meyer-Stork, L. Sebastian ; Lauter, S. L. ; Höcker, Hartwig ; Berndt, Heinz
Berndt, Heinz ; Kalbe, Jochen ; Kuropka, Rolf ; Meyer-Stork, L. Sebastian ; Sauter, S. L. ; Höcker, Hartwig
Takenaga, Shoko ; Herrera, Cony F. ; Werner, Frederik ; Biselli, Manfred ; Schnitzler, Thomas ; Schöning, Michael Josef ; Öhlschläger, Peter ; Wagner, Torsten
Meyer-Stork, L. Sebastian ; Kalbe, Jochen ; Kuropka, Rolf ; Sauter, S. L. ; Höcker, Hartwig ; Berndt, Heinz
Poly(vinyl acetate), PVAc, with a degree of polymerization Xn = 10 was prepared by chain-transfer radical polymerization using carbon tetrachloride and used as oligomeric plasticizer for commercial PVAc. However, the chlorinated chain ends cause a low thermal stability requiring mild Cl/H substitution. The product exhibits high thermal stability and excellent melt-compounding properties. Blends of oligomeric and commercial PVAc show single glass transition temperatures which decrease with higher oligomer content and exhibit small negative deviations from Fox' linear additivity rule. This indicates plasticization and miscibility being mainly due to entropic effects. Injection-moulded thick specimens show ductile behaviour at oligomer contents >10 wt %, while sheets with a thickness of 0.2–0.5 mm appear flexible already at 7.5 wt %. The oxygen permeability coefficients are an order of magnitude lower than those of low-density polyethylene. Due to the sum of their properties, the plasticized sheets present a promising alternative in the preparation of barrier materials.
Kalbe, Jochen ; Kuropka, Rolf ; Meyer-Stork, L. Sebastian ; Berndt, Heinz ; Sauter, Sybille L. ; Loss, Peter ; Hendo, Karsten ; Riesner, Detlev ; Höcker, Hartwig
Design of enzyme reactors as chromatographic columns for racemic resolution of amino acid esters
(1989)
Wiegand, Sandra ; Dietrich, Sascha ; Hertel, Robert ; Bongaerts, Johannes ; Evers, Stefan ; Volland, Sonja ; Daniel, Rolf ; Liesegang, Heiko
Size unlimited markerless deletions by a transconjugative plasmid-system in Bacillus licheniformis
(2013)
Rachinger, Michael ; Bauch, Melanie ; Strittmatter, Axel ; Bongaerts, Johannes ; Evers, Stefan ; Maurer, Karl-Heinz ; Daniel, Rolf ; Liebl, Wolfgang ; Liesegang, Heiko ; Ehrenreich, Armin
The response of Bacillus licheniformis to heat and ethanol stress and the role of the SigB regulon
(2013)
Voigt, Birgit ; Schroeter, Rebecca ; Jürgen, Britta ; Albrecht, Dirk ; Evers, Stefan ; Bongaerts, Johannes ; Maurer, Karl-Heinz ; Schweder, Thomas ; Hecker, Michael
Wilming, Anja ; Begemann, Jens ; Kuhne, Stefan ; Regestein, Lars ; Bongaerts, Johannes ; Evers, Stefan ; Maurer, Karl-Heinz ; Büchs, Jochen
Scheele, Sandra ; Oertel, Dan ; Bongaerts, Johannes ; Evers, Stefan ; Hellmuth, Hendrik ; Maurer, Karl-Heinz ; Bott, Michael ; Freudl, Roland
Disruption experiments targeted at the Bacillus licheniformis degSU operon and GFP-reporter analysis provided evidence for promoter activity immediately upstream of degU. pMutin mediated concomitant introduction of the degU32 allele – known to cause hypersecretion in Bacillus subtilis – resulted in a marked increase in protease activity. Application of 5-fluorouracil based counterselection through establishment of a phosphoribosyltransferase deficient Δupp strain eventually facilitated the marker-free introduction of degU32 leading to further protease enhancement achieving levels as for hypersecreting wild strains in which degU was overexpressed. Surprisingly, deletion of rapG – known to interfere with DegU DNA-binding in B. subtilis – did not enhance protease production neither in the wild type nor in the degU32 strain. The combination of degU32 and Δupp counterselection in the type strain is not only equally effective as in hypersecreting wild strains with respect to protease production but furthermore facilitates genetic strain improvement aiming at biological containment and effectiveness of biotechnological processes.
Bongaerts, Johannes ; Esser, Simon ; Lorbach, Volker ; Al-Momani, Lóay ; Müller, Michael A. ; Franke, Dirk ; Grondal, Christoph ; Kurutsch, Anja ; Bujnicki, Robert ; Takors, Ralf ; Raeven, Leon ; Wubbolts, Marcel ; Bovenberg, Roel ; Nieger, Martin ; Schürmann, Melanie ; Trachtmann, Natalie ; Kozak, Stefan ; Sprenger, Georg A. ; Müller, Michael
Deppe, Veronika Maria ; Klatte, Stephanie ; Bongaerts, Johannes ; Maurer, Karl-Heinz ; O'Connell, Timothy ; Meinhardt, Friedhelm
Deppe, Veronika Maria ; Bongaerts, Johannes ; O'Connell, Timothy ; Maurer, Karl-Heinz ; Meinhardt, Friedhelm
Degering, Christian ; Eggert, Thorsten ; Puls, Michael ; Bongaerts, Johannes ; Evers, Stefan ; Maurer, Karl-Heinz ; Jaeger, Karl-Erich
Bacillus subtilis and Bacillus licheniformis are widely used for the large-scale industrial production of proteins. These strains can efficiently secrete proteins into the culture medium using the general secretion (Sec) pathway. A characteristic feature of all secreted proteins is their N-terminal signal peptides, which are recognized by the secretion machinery. Here, we have studied the production of an industrially important secreted protease, namely, subtilisin BPN′ from Bacillus amyloliquefaciens. One hundred seventy-three signal peptides originating from B. subtilis and 220 signal peptides from the B. licheniformis type strain were fused to this secretion target and expressed in B. subtilis, and the resulting library was analyzed by high-throughput screening for extracellular proteolytic activity. We have identified a number of signal peptides originating from both organisms which produced significantly increased yield of the secreted protease. Interestingly, we observed that levels of extracellular protease were improved not only in B. subtilis, which was used as the screening host, but also in two different B. licheniformis strains. To date, it is impossible to predict which signal peptide will result in better secretion and thus an improved yield of a given extracellular target protein. Our data show that screening a library consisting of homologous and heterologous signal peptides fused to a target protein can identify more-effective signal peptides, resulting in improved protein export not only in the original screening host but also in different production strains.
Krämer, Marco ; Bongaerts, Johannes ; Bovenberg, Roel ; Kremer, Susanne ; Müller, Ulrike ; Orf, Sonja ; Wubbolts, Marcel ; Raeven, Leon
Gerigk, M. ; Maaß, D. ; Kreutzer, A. ; Sprenger, G. ; Bongaerts, Johannes ; Wubbolts, Marcel ; Takors, Ralf
Bongaerts, Johannes ; Bovenberg, Roel ; Krämer, Marco ; Müller, Ulrike ; Raeven, Leon ; Wubbolts, Marcel