<?xml version="1.0" encoding="ISO-8859-1"?><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">
<front>
<journal-meta>
<journal-id>2310-0265</journal-id>
<journal-title><![CDATA[Revista CON-CIENCIA]]></journal-title>
<abbrev-journal-title><![CDATA[Rev.Cs.Farm. y Bioq]]></abbrev-journal-title>
<issn>2310-0265</issn>
<publisher>
<publisher-name><![CDATA[Facultad de Ciencias Farmacéuticas y BioquímicasUniversidad Mayor de San Andrés]]></publisher-name>
</publisher>
</journal-meta>
<article-meta>
<article-id>S2310-02652024000200042</article-id>
<article-id pub-id-type="doi">10.53287/fxjx1874ur86d</article-id>
<title-group>
<article-title xml:lang="es"><![CDATA[Un estudio in silico sobre el acoplamiento molecular entre el eucaliptol y la proteasa viral MPRO/3CLPRO del SARS-CoV-2]]></article-title>
<article-title xml:lang="en"><![CDATA[In silico study on the molecular coupling between eucalyptol and the SARS-CoV-2 viral protease MPRO/3CLPRO]]></article-title>
</title-group>
<contrib-group>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Nogales Vera]]></surname>
<given-names><![CDATA[Jorge]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
<xref ref-type="aff" rid="Aaf"/>
</contrib>
<contrib contrib-type="author">
<name>
<surname><![CDATA[Choque Aspiazu]]></surname>
<given-names><![CDATA[Rigoberto]]></given-names>
</name>
<xref ref-type="aff" rid="Aff"/>
</contrib>
</contrib-group>
<aff id="Af1">
<institution><![CDATA[,aff1  ]]></institution>
<addr-line><![CDATA[ ]]></addr-line>
</aff>
<aff id="Af2">
<institution><![CDATA[,aff2  ]]></institution>
<addr-line><![CDATA[ ]]></addr-line>
</aff>
<pub-date pub-type="pub">
<day>00</day>
<month>12</month>
<year>2024</year>
</pub-date>
<pub-date pub-type="epub">
<day>00</day>
<month>12</month>
<year>2024</year>
</pub-date>
<volume>12</volume>
<numero>2</numero>
<fpage>42</fpage>
<lpage>59</lpage>
<copyright-statement/>
<copyright-year/>
<self-uri xlink:href="http://www.scielo.org.bo/scielo.php?script=sci_arttext&amp;pid=S2310-02652024000200042&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.bo/scielo.php?script=sci_abstract&amp;pid=S2310-02652024000200042&amp;lng=en&amp;nrm=iso"></self-uri><self-uri xlink:href="http://www.scielo.org.bo/scielo.php?script=sci_pdf&amp;pid=S2310-02652024000200042&amp;lng=en&amp;nrm=iso"></self-uri><abstract abstract-type="short" xml:lang="es"><p><![CDATA[Resumen  Introducción.  El presente trabajo ha estudiado el acoplamiento molecular del eucaliptol con la proteasa viral Mpro/3CLpro del SARS-CoV-2. El estudio del acoplamiento se ha utilizado diversos softwars que emplean los motores de Auto Dock Vina y sus herramientas, además de servidores en línea, de modo que se obtuvieron las conformaciones más probables en base a los parámetros: energías de enlace, RMSD, constante de disociación, eficiencia de enlace (E.L) del docking  Objetivo.  Determinar el acoplamiento molecular del eucaliptol con la proteasa viral Mpro/3CLpro del SARS-CoV-2.  Materiales y métodos.  Para realizar el acoplamiento molecular, se emplearon los softwares y servidores en línea, en cada caso se consideraron los parámetros de libre rotación de todos los enlaces del ligando con libertad conformacional, adición de cargas de Gasteiger a la proteína y al ligando, adición de hidrógenos a la proteína, generación de 100 poses para el ligando y utilización del Algoritmo Genético Lamarckiano (LGA). Este último se utilizó bajo las siguientes condiciones: 100 corridas del GA, 150 tamaño de población, 250000 máximo número de evaluaciones de energía.  Resultados.  El sitio activo en la proteasa del SARS-CoV-2 presento un volumen de 226 Å3 con las coordenadas (-13.5, 11.3, 71.6) y los siguientes aminoácidos activos: Arg 188, His 41, Pro 168, Met 49, Cys 145, Thr 190, Asp 187, Glu 166, His 164, Tyr 54, Gln 189, Met 165, Leu 167, Gln 192. Los aminoácidos encontrados en el acoplamiento involucrados en la interacción con el eucaliptol fueron Phe 140, Cys 145, His 163, His 164, Met 165, Glu 166, His 172; donde la interacción hidrofóbica es muy predominante  Conclusiones.  Existe una predominancia de fuerzas de interacción hidrofóbica intermolecular en el acoplamiento, ya que las características hidrofóbicas del sitio activo se deben a que la mayoría de los aminoácidos encontrados en este sitio activo son de carácter hidrofóbico.]]></p></abstract>
<abstract abstract-type="short" xml:lang="en"><p><![CDATA[Abstract  Introduction.  This is a study on a possible molecular coupling of eucalyptol with the viral protease Mpro/3CLpro of SARS-CoV-2. The docking required software using the Auto Dock Vina engines and its tools, as well as online servers, so that the most probable conformations were obtained based on the parameters: binding energies, RMSD, dissociation constant, binding efficiency (E.L) of docking.  Objective.  To determine molecular coupling of eucalyptol with the SARS-CoV-2 viral protease Mpro/3CLpro.  Materials and methods.  To perform the molecular docking, online software and servers were used, in each case the parameters of free rotation of all the ligand bonds with conformational freedom, addition of Gasteiger charges to the protein and the ligand, addition of hydrogens to the protein, generation of 100 poses for the ligand and use of the Lamarckian Genetic Algorithm (LGA). The latter was used under the following conditions: 100 GA runs.  Results.  The active site in the SARS Cov-2 protease had a volume of 226 Å3 with the coordinates (-13.5, 11.3, 71.6) and the following active amino acids: Arg 188, His 41, Pro 168, Met 49, Cys 145 , Thr 190, Asp 187, Glu 166, His 164, Tyr 54, Gln 189, Met 165, Leu 167, Gln 192. The amino acids found in the coupling involved in the interaction with eucalyptol were Phe 140, Cys 145, His 163, His 164, Met 165, Glu 166, His 172; where the hydrophobic interaction is very predominant.  Conclusion.  There is a predominance of intermolecular hydrophobic interaction forces in the coupling, since the hydrophobic characteristics of the active site are due to the fact that the majority of the amino acids found in this active site are hydrophobic in nature.]]></p></abstract>
<kwd-group>
<kwd lng="es"><![CDATA[Eucaliptol]]></kwd>
<kwd lng="es"><![CDATA[proteasa principal del SARS-CoV-2]]></kwd>
<kwd lng="en"><![CDATA[Eucalyptol]]></kwd>
<kwd lng="en"><![CDATA[Main protease]]></kwd>
<kwd lng="en"><![CDATA[main SARS-CoV-2 protease]]></kwd>
</kwd-group>
</article-meta>
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