Insilico Alpha-Helical Structural Recognition of Temporin Antimicrobial Peptides and Its Interactions with Middle East Respiratory Syndrome-Coronavirus
Identifieur interne : 002638 ( Ncbi/Merge ); précédent : 002637; suivant : 002639Insilico Alpha-Helical Structural Recognition of Temporin Antimicrobial Peptides and Its Interactions with Middle East Respiratory Syndrome-Coronavirus
Auteurs : Sathish Kumar Marimuthu ; Krishnanand Nagarajan ; Sathish Kumar Perumal ; Selvamani Palanisamy ; Latha SubbiahSource :
- International Journal of Peptide Research and Therapeutics [ 1573-3149 ] ; 2019.
Abstract
Many antimicrobial peptides (AMPs) have multiple antimicrobial immunity effects. One such class of peptides is temporins. Temporins are the smallest (AMPs) found in nature and are highly active against gram-positive bacteria. Nowadays, there was a rapid increase in the availability of the 3D structure of proteins in PDB (protein data bank). The conserved residues and 3D structural conformations of temporins (AMPs) were still unknown. The present study explores the sequence analysis, alpha-helical structural conformations of temporins. The sequence of temporins was deracinated from APD3 database, the three-dimensional structure was constructed by homology modeling studies. The sequence analysis results show that the conserved residues among the peptide sequences, the maximum of the sequences are 70% alike to each other. The secondary structure prediction results revealed that 99% of temporin (AMPs) exhibited in alpha-helical form. The 3D structure speculated using RAMPAGE exposes the alpha-helical conformation in all temporins (AMPs). The phylogenetic analysis reveals the evolutionary relationships of temporins (AMPs), which are branched into seven clusters. As a result, we identified a list of potential temporin AMPs which docked to the antiviral protein (MERS-CoV), it shows good protein-peptide binding. This computational approach may serve as a good model for the rationale design of temporin based antibiotics.
The online version of this article (10.1007/s10989-019-09951-y) contains supplementary material, which is available to authorized users.
Url:
DOI: 10.1007/s10989-019-09951-y
PubMed: 32206049
PubMed Central: 7088259
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<front><div type="abstract" xml:lang="en"><p id="Par1">Many antimicrobial peptides (AMPs) have multiple antimicrobial immunity effects. One such class of peptides is temporins. Temporins are the smallest (AMPs) found in nature and are highly active against gram-positive bacteria. Nowadays, there was a rapid increase in the availability of the 3D structure of proteins in PDB (protein data bank). The conserved residues and 3D structural conformations of temporins (AMPs) were still unknown. The present study explores the sequence analysis, alpha-helical structural conformations of temporins. The sequence of temporins was deracinated from APD3 database, the three-dimensional structure was constructed by homology modeling studies. The sequence analysis results show that the conserved residues among the peptide sequences, the maximum of the sequences are 70% alike to each other. The secondary structure prediction results revealed that 99% of temporin (AMPs) exhibited in alpha-helical form. The 3D structure speculated using RAMPAGE exposes the alpha-helical conformation in all temporins (AMPs). The phylogenetic analysis reveals the evolutionary relationships of temporins (AMPs), which are branched into seven clusters. As a result, we identified a list of potential temporin AMPs which docked to the antiviral protein (MERS-CoV), it shows good protein-peptide binding. This computational approach may serve as a good model for the rationale design of temporin based antibiotics.</p>
<sec><title>Electronic supplementary material</title>
<p>The online version of this article (10.1007/s10989-019-09951-y) contains supplementary material, which is available to authorized users.</p>
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<double pmid="32206049"><pmc><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Insilico Alpha-Helical Structural Recognition of Temporin Antimicrobial Peptides and Its Interactions with Middle East Respiratory Syndrome-Coronavirus</title>
<author><name sortKey="Marimuthu, Sathish Kumar" sort="Marimuthu, Sathish Kumar" uniqKey="Marimuthu S" first="Sathish Kumar" last="Marimuthu">Sathish Kumar Marimuthu</name>
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<author><name sortKey="Nagarajan, Krishnanand" sort="Nagarajan, Krishnanand" uniqKey="Nagarajan K" first="Krishnanand" last="Nagarajan">Krishnanand Nagarajan</name>
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</affiliation>
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<author><name sortKey="Perumal, Sathish Kumar" sort="Perumal, Sathish Kumar" uniqKey="Perumal S" first="Sathish Kumar" last="Perumal">Sathish Kumar Perumal</name>
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</affiliation>
</author>
<author><name sortKey="Palanisamy, Selvamani" sort="Palanisamy, Selvamani" uniqKey="Palanisamy S" first="Selvamani" last="Palanisamy">Selvamani Palanisamy</name>
<affiliation><nlm:aff id="Aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Subbiah, Latha" sort="Subbiah, Latha" uniqKey="Subbiah L" first="Latha" last="Subbiah">Latha Subbiah</name>
<affiliation><nlm:aff id="Aff1"></nlm:aff>
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<idno type="pmid">32206049</idno>
<idno type="pmc">7088259</idno>
<idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7088259</idno>
<idno type="RBID">PMC:7088259</idno>
<idno type="doi">10.1007/s10989-019-09951-y</idno>
<date when="2019">2019</date>
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<sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Insilico Alpha-Helical Structural Recognition of Temporin Antimicrobial Peptides and Its Interactions with Middle East Respiratory Syndrome-Coronavirus</title>
<author><name sortKey="Marimuthu, Sathish Kumar" sort="Marimuthu, Sathish Kumar" uniqKey="Marimuthu S" first="Sathish Kumar" last="Marimuthu">Sathish Kumar Marimuthu</name>
<affiliation><nlm:aff id="Aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Nagarajan, Krishnanand" sort="Nagarajan, Krishnanand" uniqKey="Nagarajan K" first="Krishnanand" last="Nagarajan">Krishnanand Nagarajan</name>
<affiliation><nlm:aff id="Aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Perumal, Sathish Kumar" sort="Perumal, Sathish Kumar" uniqKey="Perumal S" first="Sathish Kumar" last="Perumal">Sathish Kumar Perumal</name>
<affiliation><nlm:aff id="Aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Palanisamy, Selvamani" sort="Palanisamy, Selvamani" uniqKey="Palanisamy S" first="Selvamani" last="Palanisamy">Selvamani Palanisamy</name>
<affiliation><nlm:aff id="Aff1"></nlm:aff>
</affiliation>
</author>
<author><name sortKey="Subbiah, Latha" sort="Subbiah, Latha" uniqKey="Subbiah L" first="Latha" last="Subbiah">Latha Subbiah</name>
<affiliation><nlm:aff id="Aff1"></nlm:aff>
</affiliation>
</author>
</analytic>
<series><title level="j">International Journal of Peptide Research and Therapeutics</title>
<idno type="ISSN">1573-3149</idno>
<idno type="eISSN">1573-3904</idno>
<imprint><date when="2019">2019</date>
</imprint>
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<front><div type="abstract" xml:lang="en"><p id="Par1">Many antimicrobial peptides (AMPs) have multiple antimicrobial immunity effects. One such class of peptides is temporins. Temporins are the smallest (AMPs) found in nature and are highly active against gram-positive bacteria. Nowadays, there was a rapid increase in the availability of the 3D structure of proteins in PDB (protein data bank). The conserved residues and 3D structural conformations of temporins (AMPs) were still unknown. The present study explores the sequence analysis, alpha-helical structural conformations of temporins. The sequence of temporins was deracinated from APD3 database, the three-dimensional structure was constructed by homology modeling studies. The sequence analysis results show that the conserved residues among the peptide sequences, the maximum of the sequences are 70% alike to each other. The secondary structure prediction results revealed that 99% of temporin (AMPs) exhibited in alpha-helical form. The 3D structure speculated using RAMPAGE exposes the alpha-helical conformation in all temporins (AMPs). The phylogenetic analysis reveals the evolutionary relationships of temporins (AMPs), which are branched into seven clusters. As a result, we identified a list of potential temporin AMPs which docked to the antiviral protein (MERS-CoV), it shows good protein-peptide binding. This computational approach may serve as a good model for the rationale design of temporin based antibiotics.</p>
<sec><title>Electronic supplementary material</title>
<p>The online version of this article (10.1007/s10989-019-09951-y) contains supplementary material, which is available to authorized users.</p>
</sec>
</div>
</front>
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<pubmed><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Insilico Alpha-Helical Structural Recognition of Temporin Antimicrobial Peptides and Its Interactions with Middle East Respiratory Syndrome-Coronavirus.</title>
<author><name sortKey="Marimuthu, Sathish Kumar" sort="Marimuthu, Sathish Kumar" uniqKey="Marimuthu S" first="Sathish Kumar" last="Marimuthu">Sathish Kumar Marimuthu</name>
<affiliation><nlm:affiliation>Department of Pharmaceutical Technology, University College of Engineering, Anna University, Bharathidasan Institute of Technology (BIT) Campus, Tiruchirappalli, 620024 Tamilnadu India.</nlm:affiliation>
<wicri:noCountry code="subField">620024 Tamilnadu India</wicri:noCountry>
</affiliation>
</author>
<author><name sortKey="Nagarajan, Krishnanand" sort="Nagarajan, Krishnanand" uniqKey="Nagarajan K" first="Krishnanand" last="Nagarajan">Krishnanand Nagarajan</name>
<affiliation><nlm:affiliation>Department of Pharmaceutical Technology, University College of Engineering, Anna University, Bharathidasan Institute of Technology (BIT) Campus, Tiruchirappalli, 620024 Tamilnadu India.</nlm:affiliation>
<wicri:noCountry code="subField">620024 Tamilnadu India</wicri:noCountry>
</affiliation>
</author>
<author><name sortKey="Perumal, Sathish Kumar" sort="Perumal, Sathish Kumar" uniqKey="Perumal S" first="Sathish Kumar" last="Perumal">Sathish Kumar Perumal</name>
<affiliation><nlm:affiliation>Department of Pharmaceutical Technology, University College of Engineering, Anna University, Bharathidasan Institute of Technology (BIT) Campus, Tiruchirappalli, 620024 Tamilnadu India.</nlm:affiliation>
<wicri:noCountry code="subField">620024 Tamilnadu India</wicri:noCountry>
</affiliation>
</author>
<author><name sortKey="Palanisamy, Selvamani" sort="Palanisamy, Selvamani" uniqKey="Palanisamy S" first="Selvamani" last="Palanisamy">Selvamani Palanisamy</name>
<affiliation><nlm:affiliation>Department of Pharmaceutical Technology, University College of Engineering, Anna University, Bharathidasan Institute of Technology (BIT) Campus, Tiruchirappalli, 620024 Tamilnadu India.</nlm:affiliation>
<wicri:noCountry code="subField">620024 Tamilnadu India</wicri:noCountry>
</affiliation>
</author>
<author><name sortKey="Subbiah, Latha" sort="Subbiah, Latha" uniqKey="Subbiah L" first="Latha" last="Subbiah">Latha Subbiah</name>
<affiliation><nlm:affiliation>Department of Pharmaceutical Technology, University College of Engineering, Anna University, Bharathidasan Institute of Technology (BIT) Campus, Tiruchirappalli, 620024 Tamilnadu India.</nlm:affiliation>
<wicri:noCountry code="subField">620024 Tamilnadu India</wicri:noCountry>
</affiliation>
</author>
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<date when="2019">2019</date>
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<idno type="pmid">32206049</idno>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Insilico Alpha-Helical Structural Recognition of Temporin Antimicrobial Peptides and Its Interactions with Middle East Respiratory Syndrome-Coronavirus.</title>
<author><name sortKey="Marimuthu, Sathish Kumar" sort="Marimuthu, Sathish Kumar" uniqKey="Marimuthu S" first="Sathish Kumar" last="Marimuthu">Sathish Kumar Marimuthu</name>
<affiliation><nlm:affiliation>Department of Pharmaceutical Technology, University College of Engineering, Anna University, Bharathidasan Institute of Technology (BIT) Campus, Tiruchirappalli, 620024 Tamilnadu India.</nlm:affiliation>
<wicri:noCountry code="subField">620024 Tamilnadu India</wicri:noCountry>
</affiliation>
</author>
<author><name sortKey="Nagarajan, Krishnanand" sort="Nagarajan, Krishnanand" uniqKey="Nagarajan K" first="Krishnanand" last="Nagarajan">Krishnanand Nagarajan</name>
<affiliation><nlm:affiliation>Department of Pharmaceutical Technology, University College of Engineering, Anna University, Bharathidasan Institute of Technology (BIT) Campus, Tiruchirappalli, 620024 Tamilnadu India.</nlm:affiliation>
<wicri:noCountry code="subField">620024 Tamilnadu India</wicri:noCountry>
</affiliation>
</author>
<author><name sortKey="Perumal, Sathish Kumar" sort="Perumal, Sathish Kumar" uniqKey="Perumal S" first="Sathish Kumar" last="Perumal">Sathish Kumar Perumal</name>
<affiliation><nlm:affiliation>Department of Pharmaceutical Technology, University College of Engineering, Anna University, Bharathidasan Institute of Technology (BIT) Campus, Tiruchirappalli, 620024 Tamilnadu India.</nlm:affiliation>
<wicri:noCountry code="subField">620024 Tamilnadu India</wicri:noCountry>
</affiliation>
</author>
<author><name sortKey="Palanisamy, Selvamani" sort="Palanisamy, Selvamani" uniqKey="Palanisamy S" first="Selvamani" last="Palanisamy">Selvamani Palanisamy</name>
<affiliation><nlm:affiliation>Department of Pharmaceutical Technology, University College of Engineering, Anna University, Bharathidasan Institute of Technology (BIT) Campus, Tiruchirappalli, 620024 Tamilnadu India.</nlm:affiliation>
<wicri:noCountry code="subField">620024 Tamilnadu India</wicri:noCountry>
</affiliation>
</author>
<author><name sortKey="Subbiah, Latha" sort="Subbiah, Latha" uniqKey="Subbiah L" first="Latha" last="Subbiah">Latha Subbiah</name>
<affiliation><nlm:affiliation>Department of Pharmaceutical Technology, University College of Engineering, Anna University, Bharathidasan Institute of Technology (BIT) Campus, Tiruchirappalli, 620024 Tamilnadu India.</nlm:affiliation>
<wicri:noCountry code="subField">620024 Tamilnadu India</wicri:noCountry>
</affiliation>
</author>
</analytic>
<series><title level="j">International journal of peptide research and therapeutics</title>
<idno type="ISSN">1573-3149</idno>
<imprint><date when="2019" type="published">2019</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass></textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Many antimicrobial peptides (AMPs) have multiple antimicrobial immunity effects. One such class of peptides is temporins. Temporins are the smallest (AMPs) found in nature and are highly active against gram-positive bacteria. Nowadays, there was a rapid increase in the availability of the 3D structure of proteins in PDB (protein data bank). The conserved residues and 3D structural conformations of temporins (AMPs) were still unknown. The present study explores the sequence analysis, alpha-helical structural conformations of temporins. The sequence of temporins was deracinated from APD3 database, the three-dimensional structure was constructed by homology modeling studies. The sequence analysis results show that the conserved residues among the peptide sequences, the maximum of the sequences are 70% alike to each other. The secondary structure prediction results revealed that 99% of temporin (AMPs) exhibited in alpha-helical form. The 3D structure speculated using RAMPAGE exposes the alpha-helical conformation in all temporins (AMPs). The phylogenetic analysis reveals the evolutionary relationships of temporins (AMPs), which are branched into seven clusters. As a result, we identified a list of potential temporin AMPs which docked to the antiviral protein (MERS-CoV), it shows good protein-peptide binding. This computational approach may serve as a good model for the rationale design of temporin based antibiotics.</div>
</front>
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