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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<affiliation><nlm:affiliation>Chronic Disease Program, Regional Protein Chemistry Center, Ottawa Health Research Institute, 725 Parkdale Ave, Ottawa, Ontario K1Y 4E9, Canada.</nlm:affiliation>
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<author><name sortKey="Hao, Xiaolei" sort="Hao, Xiaolei" uniqKey="Hao X" first="Xiaolei" last="Hao">Xiaolei Hao</name>
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<author><name sortKey="Chen, Andrew" sort="Chen, Andrew" uniqKey="Chen A" first="Andrew" last="Chen">Andrew Chen</name>
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<author><name sortKey="Chretien, Michel" sort="Chretien, Michel" uniqKey="Chretien M" first="Michel" last="Chrétien">Michel Chrétien</name>
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<author><name sortKey="Basak, Ajoy" sort="Basak, Ajoy" uniqKey="Basak A" first="Ajoy" last="Basak">Ajoy Basak</name>
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<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>
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<term>Protein Structure, Tertiary</term>
<term>SARS Virus (chemistry)</term>
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<term>Sequence Analysis, Protein</term>
<term>Spectrometry, Fluorescence</term>
<term>Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization</term>
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<term>Viral Envelope Proteins (chemistry)</term>
<term>Viral Envelope Proteins (genetics)</term>
<term>Viral Envelope Proteins (metabolism)</term>
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<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>
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<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>
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<Month>12</Month>
<Day>29</Day>
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<DateRevised><Year>2019</Year>
<Month>09</Month>
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<Title>Protein and peptide letters</Title>
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<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>
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<ForeName>Sarmistha</ForeName>
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<AffiliationInfo><Affiliation>Chronic Disease Program, Regional Protein Chemistry Center, Ottawa Health Research Institute, 725 Parkdale Ave, Ottawa, Ontario K1Y 4E9, Canada.</Affiliation>
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