<!DOCTYPE article
PUBLIC "-//NLM//DTD JATS (Z39.96) Journal Publishing DTD v1.4 20190208//EN"
       "JATS-journalpublishing1.dtd">
<article xmlns:mml="http://www.w3.org/1998/Math/MathML" xmlns:xlink="http://www.w3.org/1999/xlink" xmlns:xsi="http://www.w3.org/2001/XMLSchema-instance" article-type="research-article" dtd-version="1.4" xml:lang="en">
 <front>
  <journal-meta>
   <journal-id journal-id-type="publisher-id">Russian Journal of Biological Physics and Chemisrty</journal-id>
   <journal-title-group>
    <journal-title xml:lang="en">Russian Journal of Biological Physics and Chemisrty</journal-title>
    <trans-title-group xml:lang="ru">
     <trans-title>АКТУАЛЬНЫЕ ВОПРОСЫ БИОЛОГИЧЕСКОЙ ФИЗИКИ И ХИМИИ</trans-title>
    </trans-title-group>
   </journal-title-group>
   <issn publication-format="print">2499-9962</issn>
  </journal-meta>
  <article-meta>
   <article-id pub-id-type="publisher-id">54337</article-id>
   <article-categories>
    <subj-group subj-group-type="toc-heading" xml:lang="ru">
     <subject>МЕДИЦИНСКАЯ БИОФИЗИКА И БИОФИЗИЧЕСКАЯ ХИМИЯ</subject>
    </subj-group>
    <subj-group subj-group-type="toc-heading" xml:lang="en">
     <subject>MEDICAL BIOPHYSICS AND BIOPHYSICAL CHEMISTRY</subject>
    </subj-group>
    <subj-group>
     <subject>МЕДИЦИНСКАЯ БИОФИЗИКА И БИОФИЗИЧЕСКАЯ ХИМИЯ</subject>
    </subj-group>
   </article-categories>
   <title-group>
    <article-title xml:lang="en">PEPTIDE ANTIBIOTICS - STRUCTURAL FEATURES AND REGULARITIES OF BIOLOGICAL ACTIVITY</article-title>
    <trans-title-group xml:lang="ru">
     <trans-title>ПЕПТИДНЫЕ АНТИБИОТИКИ - СТРУКТУРНЫЕ ОСОБЕННОСТИ И ЗАКОНОМЕРНОСТИ БИОЛОГИЧЕСКОЙ АКТИВНОСТИ</trans-title>
    </trans-title-group>
   </title-group>
   <contrib-group content-type="authors">
    <contrib contrib-type="author">
     <name-alternatives>
      <name xml:lang="ru">
       <surname>Рогожин</surname>
       <given-names>Е А</given-names>
      </name>
      <name xml:lang="en">
       <surname>Rogozhin</surname>
       <given-names>E A</given-names>
      </name>
     </name-alternatives>
     <email>rea21@list.ru</email>
     <xref ref-type="aff" rid="aff-1"/>
    </contrib>
   </contrib-group>
   <aff-alternatives id="aff-1">
    <aff>
     <institution xml:lang="ru">Институт биоорганической химии имени академиков М.М. Шемякина и Ю.А. Овчинникова Российской академии наук; Научно-исследовательский Институт по изысканию новых антибиотиков имени Г.Ф. Гаузе</institution>
     <country>ru</country>
    </aff>
    <aff>
     <institution xml:lang="en">Shemyakin and Ovchinnikov institute of Bioorganic Chemistry Russian Academy of Sciences; Gause Institute of New Antibiotics</institution>
     <country>ru</country>
    </aff>
   </aff-alternatives>
   <pub-date publication-format="print" date-type="pub" iso-8601-date="2018-09-25T20:22:29+03:00">
    <day>25</day>
    <month>09</month>
    <year>2018</year>
   </pub-date>
   <pub-date publication-format="electronic" date-type="pub" iso-8601-date="2018-09-25T20:22:29+03:00">
    <day>25</day>
    <month>09</month>
    <year>2018</year>
   </pub-date>
   <volume>3</volume>
   <issue>3</issue>
   <fpage>619</fpage>
   <lpage>621</lpage>
   <history>
    <date date-type="received" iso-8601-date="2018-09-20T20:22:29+03:00">
     <day>20</day>
     <month>09</month>
     <year>2018</year>
    </date>
    <date date-type="accepted" iso-8601-date="2018-09-20T20:22:29+03:00">
     <day>20</day>
     <month>09</month>
     <year>2018</year>
    </date>
   </history>
   <self-uri xlink:href="https://rusjbpc.ru/en/nauka/article/54337/view">https://rusjbpc.ru/en/nauka/article/54337/view</self-uri>
   <abstract xml:lang="ru">
    <p>В связи с широким распространением полирезистентных патогенных микроорганизмов в мировой медицинской практике высока потребность в антибиотиках, относящихся к химической группе пептидов (в частности, гликопептидов), благодаря их значительной противобактериальной активности в отношении возбудителей с множественной лекарственной устойчивостью. На данный момент в эту группу антибиотиков в номенклатуре противобактериальных медицинских препаратов входят даптомицин, рамопланин, тейкопланин и ванкомицин. Антибиотики этой группы обладают активностью в отношении грамположительных бактерий и микобактерий, в том числе и Mycobacterium tuberculosis . Преимуществом гликопептидных антибиотиков перед рядом антибиотиков других групп является бактерицидный тип действия и высокая активность в отношении микроорганизмов, устойчивых ко многим препаратам, включая β-лактамные антибиотики и фторхинолоны. По оценке Всемирной организации здравоохранения (ВОЗ), устойчивость болезнетворных микроорганизмов к антибиотикам является главным вызовом, с которым столкнулось современное здравоохранение. Проблема быстрого распространения устойчивых форм среди патогенных микроорганизмов усугубляется отсутствием у современной медицины достаточного числа эффективных антибиотиков. По данным Всемирной организации здравоохранения в период с 2000 по 2015 год в мире одобрено всего лишь 2 новых природных антибиотика для проведения клинических испытаний.</p>
   </abstract>
   <trans-abstract xml:lang="en">
    <p>Due to the wide spread of multidrug resistant pathogens in world medical practice, there is a high demand for antibiotics belonging to the chemical group of peptides (in particular, glycopeptides), due to their significant antibacterial activity against multidrug-resistant pathogens. At the moment, this group of antibiotics in the nomenclature of antibacterial medicines includes daptomycin, ramoplanin, teicoplanin and vancomycin. Antibiotics of this group have activity against gram-positive bacteria and mycobacteria, including Mycobacterium tuberculosis. The advantage of glycopeptide antibiotics over a number of antibiotics of other groups is the bactericidal type of action and high activity against microorganisms resistant to many drugs, including β-lactam antibiotics and fluoroquinolones. According to the World Health Organization (WHO), the resistance of pathogens to antibiotics is the main challenge facing modern healthcare. The problem of the rapid spread of resistant forms among pathogenic microorganisms is exacerbated by the lack of a sufficient number of effective antibiotics in modern medicine. According to the World Health Organization, from 2000 to 2015, only 2 new natural antibiotics for clinical trials have been approved worldwide.</p>
   </trans-abstract>
   <kwd-group xml:lang="ru">
    <kwd>пептидные антибиотики</kwd>
    <kwd>антимикробная активность</kwd>
    <kwd>бактериальные штаммы-продуценты</kwd>
    <kwd>структура</kwd>
   </kwd-group>
   <kwd-group xml:lang="en">
    <kwd>peptide antibiotics</kwd>
    <kwd>antimicrobial activity</kwd>
    <kwd>bacterial strains-producers</kwd>
    <kwd>structure</kwd>
   </kwd-group>
  </article-meta>
 </front>
 <body>
  <p></p>
 </body>
 <back>
  <ref-list>
   <ref id="B1">
    <label>1.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Bérdy J. Bioactive Microbial Metabolites. The Journal of Antibiotics., 2005, vol. 58, pp. 1-26.</mixed-citation>
     <mixed-citation xml:lang="en">Bérdy J. Bioactive Microbial Metabolites. The Journal of Antibiotics., 2005, vol. 58, pp. 1-26.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B2">
    <label>2.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Chin Y.-W., Balunas M.J., Chai H.B., Kinghorn A.D. Drug Discovery From Natural Sources. AAPS Journal, 2006, vol. 8, no. 2, pp. 239-253.</mixed-citation>
     <mixed-citation xml:lang="en">Chin Y.-W., Balunas M.J., Chai H.B., Kinghorn A.D. Drug Discovery From Natural Sources. AAPS Journal, 2006, vol. 8, no. 2, pp. 239-253.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B3">
    <label>3.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Hofemeister J., Conrad B., Adler B., Hofemeister B., Feesche J., Kucheryava N., Steinborn G., Franke P., Grammel N., Zwintscher A., Leenders F., Hitzeroth G, Vater J. Genetic analysis of the biosynthesis of non-ribosomal peptide- and polyketide-like antibiotics, iron uptake and biofilm formation by Bacillus subtilis A1/3. Mol. Genet. Genomics, 2004, vol. 272, pp. 363-378.</mixed-citation>
     <mixed-citation xml:lang="en">Hofemeister J., Conrad B., Adler B., Hofemeister B., Feesche J., Kucheryava N., Steinborn G., Franke P., Grammel N., Zwintscher A., Leenders F., Hitzeroth G, Vater J. Genetic analysis of the biosynthesis of non-ribosomal peptide- and polyketide-like antibiotics, iron uptake and biofilm formation by Bacillus subtilis A1/3. Mol. Genet. Genomics, 2004, vol. 272, pp. 363-378.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B4">
    <label>4.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Tamehiro N., Okamoto-Hosoya Y., Okamoto S., Ubukata M., Hamada M., Naganawa H., Ochi K. Bacilysocin, a novel phospholipid antibiotic produced by Bacillus subtilis 168. Antimicrob. Agents Chemother., 2002, vol. 46, pp. 315-320.</mixed-citation>
     <mixed-citation xml:lang="en">Tamehiro N., Okamoto-Hosoya Y., Okamoto S., Ubukata M., Hamada M., Naganawa H., Ochi K. Bacilysocin, a novel phospholipid antibiotic produced by Bacillus subtilis 168. Antimicrob. Agents Chemother., 2002, vol. 46, pp. 315-320.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B5">
    <label>5.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Zimmerman S.B., Schwartz C.D., Monaghan R.L., Pelak B.A., Weissberger B. Difficidin and oxydifficidin: novel broad spectrum antibacterial antibiotics produced by Bacillus subtilis. I. Production, taxonomy and antibacterial activity. J. Antibiot., 1987, vol. 40, pp. 1677-1681.</mixed-citation>
     <mixed-citation xml:lang="en">Zimmerman S.B., Schwartz C.D., Monaghan R.L., Pelak B.A., Weissberger B. Difficidin and oxydifficidin: novel broad spectrum antibacterial antibiotics produced by Bacillus subtilis. I. Production, taxonomy and antibacterial activity. J. Antibiot., 1987, vol. 40, pp. 1677-1681.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B6">
    <label>6.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Wilson K.E., Flor J.E., Schwartz R.E., Joshua H., Smith J.L., Pelak B.A., Liesch J.M., Hensens O.D. Difficidin and oxydifficidin: novel broad spectrum antibacterial antibiotics produced by Bacillus subtilis. II. Isolation and physic-chemical characterization. J. Antibiot., 1987, vol. 40, pp. 1682-1691.</mixed-citation>
     <mixed-citation xml:lang="en">Wilson K.E., Flor J.E., Schwartz R.E., Joshua H., Smith J.L., Pelak B.A., Liesch J.M., Hensens O.D. Difficidin and oxydifficidin: novel broad spectrum antibacterial antibiotics produced by Bacillus subtilis. II. Isolation and physic-chemical characterization. J. Antibiot., 1987, vol. 40, pp. 1682-1691.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B7">
    <label>7.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Patel P.S., Huang S., Fisher S., Pirnik D., Aklonis C., Dean L., Meyers E., Fernandes P., Mayerl F. Bacillaene, a novel inhibitor of procaryotic protein synthesis produced by Bacillus subtilis: production, taxonomy, isolation, physico-chemical characterization and biological activity. J. Antibiot., 1995, vol. 48, pp. 997-1003.</mixed-citation>
     <mixed-citation xml:lang="en">Patel P.S., Huang S., Fisher S., Pirnik D., Aklonis C., Dean L., Meyers E., Fernandes P., Mayerl F. Bacillaene, a novel inhibitor of procaryotic protein synthesis produced by Bacillus subtilis: production, taxonomy, isolation, physico-chemical characterization and biological activity. J. Antibiot., 1995, vol. 48, pp. 997-1003.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B8">
    <label>8.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Romero-Tabarez M., Jansen R., Sylla M., Lunsdorf H., Häußler S., Santosa D.A., Timmis K.N., Molinari G. 7-O-malonyl macrolactin A, a new macrolactin antibiotic from Bacillus subtilis active against methicillin-resistant Staphylococcus aureus, vancomycin-resistant Enterococci, and a small-colony variant of Burkholderia cepacia. Antimicrob. Agents Chemother., 2006, vol. 50, no. 5, pp. 1701-1709.</mixed-citation>
     <mixed-citation xml:lang="en">Romero-Tabarez M., Jansen R., Sylla M., Lunsdorf H., Häußler S., Santosa D.A., Timmis K.N., Molinari G. 7-O-malonyl macrolactin A, a new macrolactin antibiotic from Bacillus subtilis active against methicillin-resistant Staphylococcus aureus, vancomycin-resistant Enterococci, and a small-colony variant of Burkholderia cepacia. Antimicrob. Agents Chemother., 2006, vol. 50, no. 5, pp. 1701-1709.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B9">
    <label>9.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Егоров Е.С., Баранова И.Н. Бактериоцины: образование свойства, применение. Антибиотики и химиотерапия, 1999, № 6, c. 33-40. [Egorov E.S., Baranova I.N. Bacteriocins: production, properties, application. Antibiotiki I khimioterapiya, 1999, no. 6, pp. 33-40. (In Russ.)]</mixed-citation>
     <mixed-citation xml:lang="en">Egorov E.S., Baranova I.N. Bakteriociny: obrazovanie svoystva, primenenie. Antibiotiki i himioterapiya, 1999, № 6, c. 33-40. [Egorov E.S., Baranova I.N. Bacteriocins: production, properties, application. Antibiotiki I khimioterapiya, 1999, no. 6, pp. 33-40. (In Russ.)]</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B10">
    <label>10.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Rea M.C., Ross R.P., Cotter P.D., Hill C. Classification of bacteriocins from gram-positive bacteria// Prokaryotic Antimicrobial Peptides: From Genes to Applications. / Eds. Drider D., Rebuffat S. Springer Science+Business Media LLC, 2011, pp. 29-53.</mixed-citation>
     <mixed-citation xml:lang="en">Rea M.C., Ross R.P., Cotter P.D., Hill C. Classification of bacteriocins from gram-positive bacteria// Prokaryotic Antimicrobial Peptides: From Genes to Applications. / Eds. Drider D., Rebuffat S. Springer Science+Business Media LLC, 2011, pp. 29-53.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B11">
    <label>11.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Abriouel H., Franz C.M.A.P., Ben Omar N., Galvez A. Diversity and applications of Bacillus bacteriocins. FEMS Microbiol. Rev., 2011, vol. 35, pp. 201-232.</mixed-citation>
     <mixed-citation xml:lang="en">Abriouel H., Franz C.M.A.P., Ben Omar N., Galvez A. Diversity and applications of Bacillus bacteriocins. FEMS Microbiol. Rev., 2011, vol. 35, pp. 201-232.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B12">
    <label>12.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Severinov K., Semenova E., Kazakov T. Class I microcins: Their structures activities, and mechanisms of resistance. Prokaryotic Antimicrobial Peptides: From Genes to Applications. / Eds. Drider D., Rebuffat S. New York: Springer, 2011, pp. 289-308.</mixed-citation>
     <mixed-citation xml:lang="en">Severinov K., Semenova E., Kazakov T. Class I microcins: Their structures activities, and mechanisms of resistance. Prokaryotic Antimicrobial Peptides: From Genes to Applications. / Eds. Drider D., Rebuffat S. New York: Springer, 2011, pp. 289-308.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B13">
    <label>13.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Ross R.P., Morgan S., Hill C. Preservation and fermentation: past, present and future. Int. J. Food Microbiol., 2002, vol. 79, pp. 3-16.</mixed-citation>
     <mixed-citation xml:lang="en">Ross R.P., Morgan S., Hill C. Preservation and fermentation: past, present and future. Int. J. Food Microbiol., 2002, vol. 79, pp. 3-16.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B14">
    <label>14.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Yeo I., Lee N.K., Hahm Y.T. Genome sequencing of Bacillus subtilis SC-8, antagonistic to the Bacillus cereus group, isolated from traditional korean fermented-soybean food. J. Bacteriol., 2012, vol. 194, no. 2, pp. 536-537.</mixed-citation>
     <mixed-citation xml:lang="en">Yeo I., Lee N.K., Hahm Y.T. Genome sequencing of Bacillus subtilis SC-8, antagonistic to the Bacillus cereus group, isolated from traditional korean fermented-soybean food. J. Bacteriol., 2012, vol. 194, no. 2, pp. 536-537.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B15">
    <label>15.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Thimon L., Peypoux F., Wallach J., Michel G. Effect of the lipopeptide antibiotic, iturin A, on morphology and membrane ultrastruture of yeast cell. FEMS Microbiol. Lett., 1995, vol. 128, pp. 101-106.</mixed-citation>
     <mixed-citation xml:lang="en">Thimon L., Peypoux F., Wallach J., Michel G. Effect of the lipopeptide antibiotic, iturin A, on morphology and membrane ultrastruture of yeast cell. FEMS Microbiol. Lett., 1995, vol. 128, pp. 101-106.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B16">
    <label>16.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Tsuge K., Akiyama T., Shoda M. Cloning, sequencing, and characterization of the iturin A operon. J. Bacteriol., 2001, vol. 183, pp. 6265-6273.</mixed-citation>
     <mixed-citation xml:lang="en">Tsuge K., Akiyama T., Shoda M. Cloning, sequencing, and characterization of the iturin A operon. J. Bacteriol., 2001, vol. 183, pp. 6265-6273.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B17">
    <label>17.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Steller S., Vollenbroich D., Leenders F., Stein T., Conrad B., Hofemeister J., Jacques P., Thonart P., Vater J. Structural and functional organization of the fengycin synthetase multienzyme system from Bacillus subtilis b213 and A1/3. Chem. Biol., 1999, vol. 6, pp. 31-41.</mixed-citation>
     <mixed-citation xml:lang="en">Steller S., Vollenbroich D., Leenders F., Stein T., Conrad B., Hofemeister J., Jacques P., Thonart P., Vater J. Structural and functional organization of the fengycin synthetase multienzyme system from Bacillus subtilis b213 and A1/3. Chem. Biol., 1999, vol. 6, pp. 31-41.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B18">
    <label>18.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Vanittanakom N., Loeffer W., Koch U., Jung G. Fengycin - A novel antifungal lipopeptide antibiotic produced by Bacillus subtilis F-29-3. J. Antibiot., 1986, vol. 39, pp. 888-901.</mixed-citation>
     <mixed-citation xml:lang="en">Vanittanakom N., Loeffer W., Koch U., Jung G. Fengycin - A novel antifungal lipopeptide antibiotic produced by Bacillus subtilis F-29-3. J. Antibiot., 1986, vol. 39, pp. 888-901.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B19">
    <label>19.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Magnet-Dana R., Thimon L., Peypoux F., Ptak M. Surfactin/iturin A interactions may explain the synergistic effect of surfactin on the biological properties of iturin A. Biochimie, 1992, vol. 74, pp. 1047-1051.</mixed-citation>
     <mixed-citation xml:lang="en">Magnet-Dana R., Thimon L., Peypoux F., Ptak M. Surfactin/iturin A interactions may explain the synergistic effect of surfactin on the biological properties of iturin A. Biochimie, 1992, vol. 74, pp. 1047-1051.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B20">
    <label>20.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Bais H.P., Fall R., Vivanco J.M. Biocontrol of Bacillus subtilis against infection of Arabidopsis roots by Pseudomonas syringae is facilitated by biofilm formation and surfactin production. Plant Physiol., 2004, vol. 134, no. 1, pp. 307-319.</mixed-citation>
     <mixed-citation xml:lang="en">Bais H.P., Fall R., Vivanco J.M. Biocontrol of Bacillus subtilis against infection of Arabidopsis roots by Pseudomonas syringae is facilitated by biofilm formation and surfactin production. Plant Physiol., 2004, vol. 134, no. 1, pp. 307-319.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B21">
    <label>21.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Raaijmakers J.M., De Bruijn I., Nybroe O., Ongena M. Natural functions of lipopeptides from Bacillus and Pseudomonas: more than surfactants and antibiotics. FEMS Microbio.l Rev., 2010, vol. 34, no. 6, pp. 1037-1062.</mixed-citation>
     <mixed-citation xml:lang="en">Raaijmakers J.M., De Bruijn I., Nybroe O., Ongena M. Natural functions of lipopeptides from Bacillus and Pseudomonas: more than surfactants and antibiotics. FEMS Microbio.l Rev., 2010, vol. 34, no. 6, pp. 1037-1062.</mixed-citation>
    </citation-alternatives>
   </ref>
   <ref id="B22">
    <label>22.</label>
    <citation-alternatives>
     <mixed-citation xml:lang="ru">Fredenhagen A., Angst C., Peter H.H. Digestion of rhizocticins to (Z)-L-2-amino-5-phosphono-3-pentenoic acid: revision of the absolute configuration of plumbemycins A and B. J. Antibiot., 1995, vol. 48, no. 9, pp. 1043-1045.</mixed-citation>
     <mixed-citation xml:lang="en">Fredenhagen A., Angst C., Peter H.H. Digestion of rhizocticins to (Z)-L-2-amino-5-phosphono-3-pentenoic acid: revision of the absolute configuration of plumbemycins A and B. J. Antibiot., 1995, vol. 48, no. 9, pp. 1043-1045.</mixed-citation>
    </citation-alternatives>
   </ref>
  </ref-list>
 </back>
</article>
