Peptide

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Pubmed_ID Title DOI Journal
4076181 Structure of bacillomycin F, a new peptidolipid antibiotic of the iturin group 10.1111/j.1432-1033.1985.tb09307.x.

Eur J Biochem

Structure of bacillomycin F, a new peptidolipid antibiotic of the iturin group

Abstract

  • The structure of a new antibiotic of the iturin group, bacillomycin F, has been demonstrated. It is a mixture of homologous peptidolipids, essentially C51H80N12O14 and C52N82N12O14. The lipid moiety consists of minor isoC15, anteisoC15 beta-amino acids and major isoC16, isoC17 and anteisoC17 beta-amino acids. The peptide sequence was determined by studying the peptides obtained after mild HCl hydrolysis and by Edman degradation of bacillomycin F treated with N-bromosuccinimide. The sequence was confirmed by two-dimensional NMR spectrometry and fast-atom-bombardment mass spectrometry gave the molecular masses of the homologous compounds. Bacillomycin F is a cyclic peptidolipid; its complete structure is given in the paper.
4077738 Absolute configuration of the beta-hydroxyl fatty acid constituent of permetin A 10.7164/antibiotics.38.1610.

J Antibiot (Tokyo)

Absolute configuration of the beta-hydroxyl fatty acid constituent of permetin A

Abstract

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4091861 Conformation of the enkephalin cycloanalog Lys-Tyr-Gly-Gly-Phe-Leu-

None

Bioorg Khim

Conformation of the enkephalin cycloanalog Lys-Tyr-Gly-Gly-Phe-Leu-

Abstract

  • The spatial structure of an enkephaline cycloanalogue Lys-Tyr-Gly-Gly-Phe-Leu--has been investigated by means of energy calculations, fluorescence and CD-spectroscopy. Despite the high conformational mobility of the cycloanalogue, little resemblance exists between its and parent peptide's low-energy structures. Conformational factors for possible mechanisms of interaction between specific enkephalin receptors and cycloanalogue are discussed."
4126225 Properties of mutants resistant to virginiamycin

None

Arch Int Physiol Biochim

Properties of mutants resistant to virginiamycin

Abstract

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4154277 Subtilin, VI: the structure of subtilin (author's transl)

None

Hoppe Seylers Z Physiol Chem

Subtilin, VI: the structure of subtilin (author's transl)

Abstract

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4197709 Synthesis of actinomycin D lactam, 1',1'-bis(L-threo- , -diaminobutyric acid)actinomycin D 10.1021/jm00262a010.

J Med Chem

Synthesis of actinomycin D lactam, 1',1'-bis(L-threo- , -diaminobutyric acid)actinomycin D

Abstract

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4332017 Mechanism of action of bacitracin: complexation with metal ion and C 55 -isoprenyl pyrophosphate 10.1073/pnas.68.12.3223.

Proc Natl Acad Sci U S A

Mechanism of action of bacitracin: complexation with metal ion and C 55 -isoprenyl pyrophosphate

Abstract

  • The inhibition by bacitracin of the enzymatic dephosphorylation of C(55)-isoprenyl pyrophosphate is abolished by the addition of chelating agents. If, however, the chelating agent is added after a preincubation of bacitracin with a divalent cation and the lipid substrate, then its addition has little effect, indicating that bacitracin, metal ion, and C(55)-isoprenyl pyrophosphate form a complex. Various divalent cations can participate in complex formation, but monovalent cations are ineffective. A direct demonstration of the formation of a complex between the C(55)-isoprenyl pyrophosphate and bacitracin in the presence of metal ions was obtained. Molecular models that show one possible conformation for a complex between bacitracin and the C(55)-isoprenyl pyrophosphate, in which the metal ion acts as a bridge between the two compounds, are presented.
4348082 Variability of the K+-Na+ discrimination of beauvericin in mitochondrial membranes 10.1007/BF01516080.

J Bioenerg

Variability of the K+-Na+ discrimination of beauvericin in mitochondrial membranes

Abstract

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4350196 Chemical studies on tuberactinomycin. 3. The chemical structure of viomycin (tuberactinomycin B) 10.7164/antibiotics.25.427.

J Antibiot (Tokyo)

Chemical studies on tuberactinomycin. 3. The chemical structure of viomycin (tuberactinomycin B)

Abstract

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4455635 Syntheses of further analogues of norphalloin. Gly1-, L-val1- and D-Abu2-norphalloin and (beta-trideutero)-Ala5- norphalloin 10.1111/j.1399-3011.1974.tb02399.x.

Int J Pept Protein Res

Syntheses of further analogues of norphalloin. Gly1-, L-val1- and D-Abu2-norphalloin and (beta-trideutero)-Ala5- norphalloin

Abstract

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4528068 The structure and synthesis of malformin A 10.1073/pnas.71.7.2791.

Proc Natl Acad Sci U S A

The structure and synthesis of malformin A

Abstract

  • A structure (the disulfide form of cyclo-D-cysteinyl-L-valyl-D-cysteinyl-D-leucyl-L-isoleucyl), previously proposed for malformin A, was reexamined. On the basis of chemical degradations, a different structure (the disulfide form of cyclo-D-cysteinyl-D-cysteinyl-L-valyl-D-leucyl-L-isoleucyl) was established. Accordingly, a compound with this structure was synthesized and was found to be identical with malformin A. The synthetic product causes curvatures on corn roots; maximum effect was seen at a concentration of 0.1 mug/ml, the optimal concentration for malformin A.
4591125 The action of serratamolide on ion movement in lipid bilayers and biomembranes 10.1016/0005-2736(73)90224-1.

Biochim Biophys Acta

The action of serratamolide on ion movement in lipid bilayers and biomembranes

Abstract

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4613708 Metabolites of microorganisms. 143. Echinocandin B, a novel polypeptide-antibiotic from Aspergillus nidulans var. echinulatus: isolation and structural components 10.1002/hlca.19740570818.

Helv Chim Acta

Metabolites of microorganisms. 143. Echinocandin B, a novel polypeptide-antibiotic from Aspergillus nidulans var. echinulatus: isolation and structural components

Abstract

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4691054 Cannabis debate continued

None

Br Med J

Cannabis debate continued

Abstract

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4857466 Isolation and structural clarification of chlamydocin 10.1002/hlca.19740570306.

Helv Chim Acta

Isolation and structural clarification of chlamydocin

Abstract

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