[Isolation, biological properties, and spatial structure of an antibiotic loloatin A]

S A Krachkovskiĭ; A G Sobol'; T V Ovchinnikova; A A Tagaev; Z A Iakimenko; R R Azizbekian; N I Kuznetsova; T N Shamshina; A S Arsen'ev

doi:10.1023/a:1019531505769

[Isolation, biological properties, and spatial structure of an antibiotic loloatin A]

Bioorg Khim. 2002 Jul-Aug;28(4):298-302. doi: 10.1023/a:1019531505769.

[Article in Russian]

Authors

S A Krachkovskiĭ¹, A G Sobol', T V Ovchinnikova, A A Tagaev, Z A Iakimenko, R R Azizbekian, N I Kuznetsova, T N Shamshina, A S Arsen'ev

Affiliation

¹ Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences, ul. Miklukho-Maklaya 16/10, GSP Moscow, 117997 Russia.

PMID: 12197385
DOI: 10.1023/a:1019531505769

Abstract

Peptide antibiotic with cyanolytic activity was isolated from the IGM52 strain of the Brevibacillus laterosporus Gram-positive spore-forming bacteria. By 1H NMR spectroscopy, this antibiotic was identified as loloatin A, a cyclic decapeptide cyclo(-Asn-Asp-Tyr-Val-Orn-Leu-DTyr-Pro-Phe-DPhe-). The spatial structure of loloatin A in solution was determined. The English version of the paper: Russian Journal of Bioorganic Chemistry, 2002, vol. 28, no. 4; see also http://www.maik.ru.

MeSH terms

Amino Acid Sequence
Anti-Bacterial Agents / chemistry
Anti-Bacterial Agents / isolation & purification*
Anti-Bacterial Agents / pharmacology
Bacillus / chemistry*
Cyanobacteria / drug effects
Magnetic Resonance Spectroscopy
Models, Molecular
Peptides, Cyclic / chemistry
Peptides, Cyclic / isolation & purification*
Peptides, Cyclic / pharmacology
Protein Conformation

Substances

Anti-Bacterial Agents
Peptides, Cyclic