Structural and biochemical investigation of heptad repeat derived peptides of human SARS corona virus (hSARS-CoV) spike protein.
Identifieur interne : 000D41 ( PubMed/Corpus ); précédent : 000D40; suivant : 000D42Structural and biochemical investigation of heptad repeat derived peptides of human SARS corona virus (hSARS-CoV) spike protein.
Auteurs : Sarmistha Basak ; Xiaolei Hao ; Andrew Chen ; Michel Chrétien ; Ajoy BasakSource :
- Protein and peptide letters [ 0929-8665 ] ; 2008.
English descriptors
- KwdEn :
- Amino Acid Sequence, Chromatography, High Pressure Liquid, Circular Dichroism, Electrophoresis, Polyacrylamide Gel, Mass Spectrometry, Membrane Fusion Proteins, Membrane Glycoproteins (chemistry), Membrane Glycoproteins (genetics), Membrane Glycoproteins (metabolism), Peptides (chemical synthesis), Peptides (chemistry), Peptides (metabolism), Protein Binding, Protein Denaturation, Protein Structure, Secondary, Protein Structure, Tertiary, SARS Virus (chemistry), SARS Virus (metabolism), Sequence Analysis, Protein, Spectrometry, Fluorescence, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, Spike Glycoprotein, Coronavirus, Viral Envelope Proteins (chemistry), Viral Envelope Proteins (genetics), Viral Envelope Proteins (metabolism).
- MESH :
- chemical , chemical synthesis : Peptides.
- chemical , chemistry : Membrane Glycoproteins, Peptides, Viral Envelope Proteins.
- chemical , genetics : Membrane Glycoproteins, Viral Envelope Proteins.
- chemical , metabolism : Membrane Glycoproteins, Peptides, Viral Envelope Proteins.
- chemical : Membrane Fusion Proteins, Spike Glycoprotein, Coronavirus.
- chemistry : SARS Virus.
- metabolism : SARS Virus.
- Amino Acid Sequence, Chromatography, High Pressure Liquid, Circular Dichroism, Electrophoresis, Polyacrylamide Gel, Mass Spectrometry, Protein Binding, Protein Denaturation, Protein Structure, Secondary, Protein Structure, Tertiary, Sequence Analysis, Protein, Spectrometry, Fluorescence, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization.
Abstract
hSARS-CoV is the causative agent for SARS infection. Its spike glycoprotein (S) is processed by host furin enzyme to produce S1 and S2 fragments, the latter being crucial for fusion with the host membrane. This takes place via formation of a coiled coil 6-helix bundle involving N and C-terminal heptad repeat domains (HR-N and HR-C) of S2. Several fluorescent and non-fluorescent peptides from these domains were synthesized to examine their interactions by circular dichroism, thermal denaturation, native-page, mass spectrometry and fluorescence spectroscopy studies. Data revealed that HR-C domains (1153-1189), (1153-1172) and (1164-1184) all exhibit potent binding interactions with HR-N(892-931) domain. These peptides may find useful therapeutic applications in SARS intervention.
DOI: 10.2174/092986608785849173
PubMed: 18991761
Links to Exploration step
pubmed:18991761Le document en format XML
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sort="Basak, Ajoy" uniqKey="Basak A" first="Ajoy" last="Basak">Ajoy Basak</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2008">2008</date><idno type="RBID">pubmed:18991761</idno><idno type="pmid">18991761</idno><idno type="doi">10.2174/092986608785849173</idno><idno type="wicri:Area/PubMed/Corpus">000D41</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000D41</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Structural and biochemical investigation of heptad repeat derived peptides of human SARS corona virus (hSARS-CoV) spike protein.</title><author><name sortKey="Basak, Sarmistha" sort="Basak, Sarmistha" uniqKey="Basak S" first="Sarmistha" last="Basak">Sarmistha Basak</name><affiliation><nlm:affiliation>Chronic Disease Program, Regional Protein Chemistry Center, Ottawa Health Research Institute, 725 Parkdale Ave, Ottawa, Ontario K1Y 4E9, Canada.</nlm:affiliation></affiliation></author><author><name sortKey="Hao, Xiaolei" sort="Hao, Xiaolei" uniqKey="Hao X" first="Xiaolei" last="Hao">Xiaolei Hao</name></author><author><name sortKey="Chen, Andrew" sort="Chen, Andrew" uniqKey="Chen A" first="Andrew" last="Chen">Andrew Chen</name></author><author><name sortKey="Chretien, Michel" sort="Chretien, Michel" uniqKey="Chretien M" first="Michel" last="Chrétien">Michel Chrétien</name></author><author><name sortKey="Basak, Ajoy" sort="Basak, Ajoy" uniqKey="Basak A" first="Ajoy" last="Basak">Ajoy Basak</name></author></analytic><series><title level="j">Protein and peptide letters</title><idno type="ISSN">0929-8665</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Chromatography, High Pressure Liquid</term><term>Circular Dichroism</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Mass Spectrometry</term><term>Membrane Fusion Proteins</term><term>Membrane Glycoproteins (chemistry)</term><term>Membrane Glycoproteins (genetics)</term><term>Membrane Glycoproteins (metabolism)</term><term>Peptides (chemical synthesis)</term><term>Peptides (chemistry)</term><term>Peptides (metabolism)</term><term>Protein Binding</term><term>Protein Denaturation</term><term>Protein Structure, Secondary</term><term>Protein Structure, Tertiary</term><term>SARS Virus (chemistry)</term><term>SARS Virus (metabolism)</term><term>Sequence Analysis, Protein</term><term>Spectrometry, Fluorescence</term><term>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</term><term>Spike Glycoprotein, Coronavirus</term><term>Viral Envelope Proteins (chemistry)</term><term>Viral Envelope Proteins (genetics)</term><term>Viral Envelope Proteins (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemical synthesis" xml:lang="en"><term>Peptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Membrane Glycoproteins</term><term>Peptides</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Membrane Glycoproteins</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Membrane Glycoproteins</term><term>Peptides</term><term>Viral Envelope Proteins</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Membrane Fusion Proteins</term><term>Spike Glycoprotein, Coronavirus</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Chromatography, High Pressure Liquid</term><term>Circular Dichroism</term><term>Electrophoresis, Polyacrylamide Gel</term><term>Mass Spectrometry</term><term>Protein Binding</term><term>Protein Denaturation</term><term>Protein Structure, Secondary</term><term>Protein Structure, Tertiary</term><term>Sequence Analysis, Protein</term><term>Spectrometry, Fluorescence</term><term>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">hSARS-CoV is the causative agent for SARS infection. Its spike glycoprotein (S) is processed by host furin enzyme to produce S1 and S2 fragments, the latter being crucial for fusion with the host membrane. This takes place via formation of a coiled coil 6-helix bundle involving N and C-terminal heptad repeat domains (HR-N and HR-C) of S2. Several fluorescent and non-fluorescent peptides from these domains were synthesized to examine their interactions by circular dichroism, thermal denaturation, native-page, mass spectrometry and fluorescence spectroscopy studies. Data revealed that HR-C domains (1153-1189), (1153-1172) and (1164-1184) all exhibit potent binding interactions with HR-N(892-931) domain. These peptides may find useful therapeutic applications in SARS intervention.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18991761</PMID><DateCompleted><Year>2008</Year><Month>12</Month><Day>29</Day></DateCompleted><DateRevised><Year>2019</Year><Month>09</Month><Day>11</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0929-8665</ISSN><JournalIssue CitedMedium="Print"><Volume>15</Volume><Issue>9</Issue><PubDate><Year>2008</Year></PubDate></JournalIssue><Title>Protein and peptide letters</Title><ISOAbbreviation>Protein Pept. Lett.</ISOAbbreviation></Journal><ArticleTitle>Structural and biochemical investigation of heptad repeat derived peptides of human SARS corona virus (hSARS-CoV) spike protein.</ArticleTitle><Pagination><MedlinePgn>874-86</MedlinePgn></Pagination><Abstract><AbstractText>hSARS-CoV is the causative agent for SARS infection. Its spike glycoprotein (S) is processed by host furin enzyme to produce S1 and S2 fragments, the latter being crucial for fusion with the host membrane. This takes place via formation of a coiled coil 6-helix bundle involving N and C-terminal heptad repeat domains (HR-N and HR-C) of S2. Several fluorescent and non-fluorescent peptides from these domains were synthesized to examine their interactions by circular dichroism, thermal denaturation, native-page, mass spectrometry and fluorescence spectroscopy studies. Data revealed that HR-C domains (1153-1189), (1153-1172) and (1164-1184) all exhibit potent binding interactions with HR-N(892-931) domain. These peptides may find useful therapeutic applications in SARS intervention.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Basak</LastName><ForeName>Sarmistha</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Chronic Disease Program, Regional Protein Chemistry Center, Ottawa Health Research Institute, 725 Parkdale Ave, Ottawa, Ontario K1Y 4E9, Canada.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Hao</LastName><ForeName>Xiaolei</ForeName><Initials>X</Initials></Author><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Andrew</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Chrétien</LastName><ForeName>Michel</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Basak</LastName><ForeName>Ajoy</ForeName><Initials>A</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Protein Pept Lett</MedlineTA><NlmUniqueID>9441434</NlmUniqueID><ISSNLinking>0929-8665</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D050576">Membrane Fusion Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D008562">Membrane Glycoproteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010455">Peptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D064370">Spike Glycoprotein, Coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014759">Viral Envelope Proteins</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002851" MajorTopicYN="N">Chromatography, High Pressure Liquid</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002942" MajorTopicYN="N">Circular Dichroism</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004591" MajorTopicYN="N">Electrophoresis, Polyacrylamide Gel</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013058" MajorTopicYN="N">Mass Spectrometry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D050576" MajorTopicYN="N">Membrane Fusion Proteins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008562" MajorTopicYN="N">Membrane Glycoproteins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010455" MajorTopicYN="N">Peptides</DescriptorName><QualifierName UI="Q000138" MajorTopicYN="N">chemical synthesis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011489" MajorTopicYN="N">Protein Denaturation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017433" MajorTopicYN="N">Protein Structure, Secondary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName 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