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 <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">54243</article-id>
   <article-categories>
    <subj-group subj-group-type="toc-heading" xml:lang="ru">
     <subject>Общая биофизика</subject>
    </subj-group>
    <subj-group subj-group-type="toc-heading" xml:lang="en">
     <subject>General biophysics</subject>
    </subj-group>
    <subj-group>
     <subject>Общая биофизика</subject>
    </subj-group>
   </article-categories>
   <title-group>
    <article-title xml:lang="en">MODIFICATION OF GREEN FLUORESCENT PROTEIN FOR SYNTHESIS OF ANTIMICROBIAL PEPTIDES</article-title>
    <trans-title-group xml:lang="ru">
     <trans-title>МОДИФИКАЦИЯ ЗЕЛЕНОГО ФЛУОРЕСЦЕНТНОГО БЕЛКА ДЛЯ СИНТЕЗА АНТИМИКРОБНЫХ ПЕПТИДОВ</trans-title>
    </trans-title-group>
   </title-group>
   <contrib-group content-type="authors">
    <contrib contrib-type="author">
     <name-alternatives>
      <name xml:lang="ru">
       <surname>Глухова</surname>
       <given-names>К А</given-names>
      </name>
      <name xml:lang="en">
       <surname>Glukhova</surname>
       <given-names>K A</given-names>
      </name>
     </name-alternatives>
     <email>gkseniya@gmail.com</email>
     <xref ref-type="aff" rid="aff-1"/>
    </contrib>
    <contrib contrib-type="author">
     <name-alternatives>
      <name xml:lang="ru">
       <surname>Кляшторный</surname>
       <given-names>В Г</given-names>
      </name>
      <name xml:lang="en">
       <surname>Kljashtorny</surname>
       <given-names>V G</given-names>
      </name>
     </name-alternatives>
     <xref ref-type="aff" rid="aff-2"/>
    </contrib>
    <contrib contrib-type="author">
     <name-alternatives>
      <name xml:lang="ru">
       <surname>Мельник</surname>
       <given-names>Б С</given-names>
      </name>
      <name xml:lang="en">
       <surname>Melnik</surname>
       <given-names>B S</given-names>
      </name>
     </name-alternatives>
     <xref ref-type="aff" rid="aff-3"/>
    </contrib>
   </contrib-group>
   <aff-alternatives id="aff-1">
    <aff>
     <institution xml:lang="ru">Институт белка РАН</institution>
     <country>ru</country>
    </aff>
    <aff>
     <institution xml:lang="en">Institute of protein research RAS</institution>
     <country>ru</country>
    </aff>
   </aff-alternatives>
   <aff-alternatives id="aff-2">
    <aff>
     <institution xml:lang="ru">Институт белка РАН</institution>
     <country>ru</country>
    </aff>
    <aff>
     <institution xml:lang="en">Institute of protein research RAS</institution>
     <country>ru</country>
    </aff>
   </aff-alternatives>
   <aff-alternatives id="aff-3">
    <aff>
     <institution xml:lang="ru">Институт белка РАН</institution>
     <country>ru</country>
    </aff>
    <aff>
     <institution xml:lang="en">Institute of protein research RAS</institution>
     <country>ru</country>
    </aff>
   </aff-alternatives>
   <pub-date publication-format="print" date-type="pub" iso-8601-date="2018-03-25T20:22:29+03:00">
    <day>25</day>
    <month>03</month>
    <year>2018</year>
   </pub-date>
   <pub-date publication-format="electronic" date-type="pub" iso-8601-date="2018-03-25T20:22:29+03:00">
    <day>25</day>
    <month>03</month>
    <year>2018</year>
   </pub-date>
   <volume>3</volume>
   <issue>1</issue>
   <fpage>46</fpage>
   <lpage>50</lpage>
   <history>
    <date date-type="received" iso-8601-date="2018-03-20T20:22:29+03:00">
     <day>20</day>
     <month>03</month>
     <year>2018</year>
    </date>
    <date date-type="accepted" iso-8601-date="2018-03-20T20:22:29+03:00">
     <day>20</day>
     <month>03</month>
     <year>2018</year>
    </date>
   </history>
   <self-uri xlink:href="https://rusjbpc.ru/en/nauka/article/54243/view">https://rusjbpc.ru/en/nauka/article/54243/view</self-uri>
   <abstract xml:lang="ru">
    <p>В настоящее время антимикробные пептиды являются конкурентоспособной альтернативой классическим антибиотикам. Их широкое использование ограничивается рядом проблем, связанных с наработкой токсичных пептидов в клетках E. coli и их доставкой в целевой сайт в организме. В данной работе проверена идея, которая помогла бы решить эти проблемы. Мы предположили, что зеленый флуоресцентный белок можно использовать как контейнер для «хранения» антибактериального пептида. Изначально, внутри бочонка зеленого флуоресцентного белка «спрятана» альфа-спираль, на которой образуется хромофор. В самой альфа-спирали есть гидрофильные аминокислоты, рядом, в середине бочонка, множество молекул связанной воды. Поэтому, мы предположили, что центральная альфа-спираль зеленого флуоресцентного белка может быть заменена на альфа-спиральный антибактериальный пептид. Реализация такой идеи достаточно сложна и на первом этапе возникают несколько вопросов, без ответа на которые невозможна дальнейшая работа в намеченном направлении. Будет ли зеленый флуоресцентный белок с замененной альфа-спиралью сворачиваться? Возможно ли при этом образование хромофора? Токсична ли такая конструкция для клетки? В данной работе была выполнена модификация зеленого флуоресцентного белка. Центральная альфа-спираль была заменена на последовательность антимикробного пептида бактенецина. Результаты наших экспериментов показывают, что такой химерный (мутантный) белок компактен, растворим, не токсичен для клетки. Однако он сильно дестабилизирован, вероятно, поэтому не образуется хромофор. Полученные результаты показывают, что идея об использовании зеленого флуоресцентного белка как «контейнера» для небольших пептидов вполне может быть реализована.</p>
   </abstract>
   <trans-abstract xml:lang="en">
    <p>At present antimicrobial peptides are a competitive alternative to classic antibiotics. Their wide use is limited to a number of problems associated with the generation of toxic peptides in E. coli cells and their delivery to the target site in the organism. We have verified the idea that could help solving this problem. We proposed that green fluorescent protein can be used as a container for “storage” of an antibacterial peptide. An alpha-helix on which a chromophore is formed is initially “hidden” inside the barrel of green fluorescent protein. The alpha-helix itself contains hydrophobic amino acids, and nearby in the center of the barrel there are many bound water molecules. Therefore we suggested that the central alpha-helix of green fluorescent protein can be substituted for an antibacterial peptide. It is rather difficult to realize this idea, and at the first stage there appear several issues without solving which it is impossible to continue the studies as required. Will green fluorescent protein with the substituted alpha-helix fold? Can the chromophore be formed in this case? Is this construction toxic to the cell? We modified green fluorescent protein. The central alpha-helix was substituted by the sequence of antimicrobial peptide bactenecin. The results of our experiments show that such a chimera (mutant) protein is compact, soluble, nontoxic to the cell. However it is strongly destabilized, which may be a reason why the chromophore is not formed. Our results demonstrate that the idea to use green fluorescent protein as a “container” for small peptides is quite realizable.</p>
   </trans-abstract>
   <kwd-group xml:lang="ru">
    <kwd>зеленый флуоресцентный белок</kwd>
    <kwd>антимикробные пептиды</kwd>
    <kwd>бактенецин</kwd>
    <kwd>молекулярная динамика</kwd>
   </kwd-group>
   <kwd-group xml:lang="en">
    <kwd>green fluorescent protein</kwd>
    <kwd>antibacterial peptides</kwd>
    <kwd>bactenecin</kwd>
    <kwd>molecular dynamics</kwd>
   </kwd-group>
  </article-meta>
 </front>
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