Total synthesis of the antibiotic polymyxin B1

Vogler, K.; Studer, R. O.; Lanz, P.; Lergier, W.; Böhni, E.

doi:10.1007/bf02147959

Cited by 29 publications

(17 citation statements)

References 10 publications

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“…A2bu, 2,4-diaminobutyric acid; CMC, critical micel-ranalexin in the presence of trifluoroethanol, a well-known helix lar concentration; CSI, chemical shift index ; DodPCho, dodecylphosinducer, and in the presence of micelles assumed to mimic a phocholine; ( 2 H38)DodPCho, perdeuterated dodecylphosphocholine; membranous environment. Since the macrocycle is a prerequi-DQF-COSY, two-dimensional double-quantum filtered correlation site for antimicrobial activity in polymyxin A [19,20] and since spectroscopy; MBC, minimal bactericidal concentration; Me2SO, the Cys20 deletion induces a decrease in antimicrobial activity dimethylsulfoxide; MIC, minimal inhibitory concentration; RnxSH, reduced form of ranalexin; RnxSS, oxidised form of ranalexin.of ranalexin [16], we evaluated the role of the disulphide bond …”

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confidence: 99%

“…Both the macrocycle size and the cationic residues are important for the biological activity of polyThe skin of some amphibians is rich in antimicrobial peptides [2, 14,15]. More than 15 antibacterial peptides have been myxin A [19,20]. By comparison of the sequences of the two macrocycles, it appears that residues T17, K18 and K19 in ranaisolated from Xenopus laevis, Bombina sp.…”

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confidence: 99%

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Solution structure of the antimicrobial peptide ranalexin and a study of its interaction with perdeuterated dodecylphosphocholine micelles

Vignal

Chavanieu

Roch

et al. 1998

European Journal of Biochemistry

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Ranalexin, a 20-residue peptide isolated from the skin of the bullfrog Rana catesbeiana displays antimicrobial activity. This peptide contains two cysteine residues in positions 14 and 20 linked by a disulphide bridge. Ranalexin was chemically synthesised and close antimicrobial activities were measured for the reduced and oxidised forms. The solution structure of ranalexin was determined by using circular dichroism, proton NMR spectroscopy and molecular modelling techniques. The reduced and oxidised forms of ranalexin are mainly unstructured in water but display an A-helical structure spanning residues 8Ϫ15 and 8Ϫ17, respectively, in a trifluoroethanol/water mixture (3:7, by vol.). Ranalexin was found to interact with micelles of dodecylphosphocholine and to adopt a similar helical structure. Moreover, slowexchanging amide protons located on the same side of the helix suggest that the hydrophobic face of the helix lies on the micelle surface. Hydrophobic residues of the poorly structured N-terminal part which are important for the biological activity are also involved in the interaction with micelles. Taken together, the results suggest that the disulphide bond does not strongly affect either the conformation or the antimicrobial activity of ranalexin.Keywords : A-helix; antimicrobial; micelle; ranalexin; NMR.Based on their structure, host defense peptides can be di-ing to a heptapeptide macrocycle. Similar macrocycles are also observed in the antimicrobial peptides belonging to the brevinin vided into two classes: linear peptides and cyclic peptides with one to three disulphide bonds. Most of these peptides have the [17] and gaegurin families [18]. A sequence alignment for ranalexin, brevinin-1 and gaegurin-5 and 6 is proposed in Fig. 1. common feature of being highly basic and of forming amphipathic structures [1]. Members of the first class include magai-Ranalexin was found to share structural similarities with polymyxin A, a well-known antimicrobial pseudo-peptide isolated nins [2, 3] and cecropins [4Ϫ6]. Members of the second class include mammalian defensins [7Ϫ9] as well as insect defensins 50 years ago. The two molecules display a heptapeptide macrocycle due to a disulphide linkage in ranalexin and to an amide [10Ϫ12]. These peptides contain six cysteines forming three disulphide bonds [13].linkage in polymyxin A. Both the macrocycle size and the cationic residues are important for the biological activity of polyThe skin of some amphibians is rich in antimicrobial peptides [2,14,15]. More than 15 antibacterial peptides have been myxin A [19,20]. By comparison of the sequences of the two macrocycles, it appears that residues T17, K18 and K19 in ranaisolated from Xenopus laevis, Bombina sp. and Phyllomedusa sp. These molecules are produced and stored in specialised der-lexin correspond to residues T7, A 2 bu8 and A 2 bu9 in polymyxin A [A 2bu (2,4-diaminobutyric acid) is positively charged] [16]. mic structures called granular glands which liberate their content during adrenergic stimulation or as the re...

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confidence: 99%

mentioning

confidence: 99%

Solution structure of the antimicrobial peptide ranalexin and a study of its interaction with perdeuterated dodecylphosphocholine micelles

Vignal

Chavanieu

Roch

et al. 1998

European Journal of Biochemistry

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“…1, these peptides differ only in the amino acid residues at positions three, six, and seven, and in the nature of the amino-terminal fatty acid. The structures of polymyxin Bl (VOGLER et al, 1964) and of circulin A (STUDER et al, 1966) have been confirmed by chemical synthesis. Previous structures proposed for these peptides (BISERTE and DAUTREVAUX, 1957;SUZUKI, 1957;DAUTREVAUX and BISERTE, 1961;KOFFLER and KOBAYASHI, 1959) appear to be incorrect.…”

Section: Polymyxins Henry Paulusmentioning

confidence: 83%

“…However it was shown subsequently that polymyxin B contains only L-DBA WILKINSON and LOWE, 1964a;VOGLER et al, 1964), and the results of PAULUS and GRAY must therefore be re-examined. Since they had not analyzed the distribution of radioactivity in the polymyxin produced in these experiments, the possibility that DBA-HC had contributed radioactivity to the other amino acid residues of polymyxin, such as threonine, cannot be eliminated.…”

Section: Henry Paulusmentioning

confidence: 93%

Biosynthesis

1967

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All rights, especially that of translation into f oreign 1anguages, reserved. It is also forbidden to reproduce this book, either who1e or in part, by photomechanical means (photostat, microfilm and/or microcard) or by other procedure without written pennission from Springcr-Vcrlag Berlin Heide1bCig GmbH. DedicationFor most areas of scientific pursuit, there is usually that rare investigator who has the imagination to conceive ideas, who has faith in his visions, and who has the ability to critically test his concepts in the laboratory. Almost invariably, this scientist also inspires younger men to enthusiastically enter into his research program. To him should go the accolades and the recognitions of the esteem in which he is held. As only a small part of this esteem, we wish to dedicate these books to Professor SELMAN A. W AKSMAN in appreciation of his leadership and contributions in all facets of antibiotic research. PrefaceThe idea for publishing these books on the mechanism of action and on the biosynthesis of antibiotics was born of frustration in our attempts to keep abreast of the literature. Gone were the years when we were able to keep a bibliography on antibiotics and feel confident that we could find everything that was being published on this sUbject. These fields of investigation were moving forward so rapidly and were encompassing so wide a range of specialized areas in microbiology and chemistry that it was almost impossible to keep abreast of developments. In our naivete and enthusiasm, however, we were unaware that we were toying with an idea that might enmesh us, that we were creating an entity with a life of its own, that we were letting loose a Golom who instead of being our servant would be our master.That we set up ideals for these books is obvious; they would be current guides to developments and information in the areas of mechanism of action and biosynthesis of antibiotics. For almost every subject, we wished to enlist the aid of an investigator who himself had played a part in determining the nature of the phenomena that were being discussed. One concept for the books was that they include only antibiotics for which a definitive, well-documented mechanism of action or biosynthetic pathway was known. Yet, such an approach would not entirely serve the purpose we projected, for it would not encompass all of the information available in these fields of antibiotic investigations and blind searches for the original literature would still have to be made. We therefore chose to include any and all antibiotics about which some pertinent information had been published. It was obvious even at the start that such a compilation, integration, and analysis of information could never be complete unless scientific investigations ceased at the moment the last manuscript was submitted-an end that was neither desirable nor possible. An addendum was therefore included at the end of the volume and left open for the addition of new information until the last pages of the regular articles had been printed.The...

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“…Aus dem Cyclisierungsprodukt wurden die restlichen Schutzgruppen durch Natrium in fliissigem Ammoniak entfernt. Anschliessend erfolgte die Reinigung dieses Roliproduktes durch Gegenstromverteilung im System ~~-13utanol/Pyridin/Eisessig/Was-ser ( [15] besonders wichtig waren, zeigen vollige Ubereinstimmung (Fig. 4).…”

unclassified

Synthesen in der Polymyxinreihe. 10. Mitteilung. Die Synthese von Colistin A (Polymyxin E₁)

Studer¹,

Lergier²,

Lanz³

et al. 1965

Helvetica Chimica Acta

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Total synthesis of the antibiotic polymyxin B1

Cited by 29 publications

References 10 publications

Solution structure of the antimicrobial peptide ranalexin and a study of its interaction with perdeuterated dodecylphosphocholine micelles

Solution structure of the antimicrobial peptide ranalexin and a study of its interaction with perdeuterated dodecylphosphocholine micelles

Biosynthesis

Synthesen in der Polymyxinreihe. 10. Mitteilung. Die Synthese von Colistin A (Polymyxin E₁)

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Total synthesis of the antibiotic polymyxin B1

Cited by 29 publications

References 10 publications

Solution structure of the antimicrobial peptide ranalexin and a study of its interaction with perdeuterated dodecylphosphocholine micelles

Solution structure of the antimicrobial peptide ranalexin and a study of its interaction with perdeuterated dodecylphosphocholine micelles

Biosynthesis

Synthesen in der Polymyxinreihe. 10. Mitteilung. Die Synthese von Colistin A (Polymyxin E1)

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Synthesen in der Polymyxinreihe. 10. Mitteilung. Die Synthese von Colistin A (Polymyxin E₁)