Molecular-level understanding of the adsorption mechanism of a graphite-binding peptide at the water/graphite interface.
Identifieur interne : 002905 ( Main/Exploration ); précédent : 002904; suivant : 002906Molecular-level understanding of the adsorption mechanism of a graphite-binding peptide at the water/graphite interface.
Auteurs : M J Penna [Australie] ; M. Mijajlovic ; C. Tamerler ; M J BiggsSource :
- Soft matter [ 1744-6848 ] ; 2015.
Descripteurs français
- KwdFr :
- Adsorption (MeSH), Conformation des protéines (MeSH), Diffusion (MeSH), Eau (composition chimique), Graphite (composition chimique), Interactions hydrophobes et hydrophiles (MeSH), Liaison hydrogène (MeSH), Peptides (composition chimique), Propriétés de surface (MeSH), Simulation de dynamique moléculaire (MeSH), Thermodynamique (MeSH).
- MESH :
English descriptors
- KwdEn :
- MESH :
Abstract
The association of proteins and peptides with inorganic material has vast technological potential. An understanding of the adsorption of peptides at liquid/solid interfaces on a molecular-level is fundamental to fully realising this potential. Combining our prior work along with the statistical analysis of 100+ molecular dynamics simulations of adsorption of an experimentally identified graphite binding peptide, GrBP5, at the water/graphite interface has been used here to propose a model for the adsorption of a peptide at a liquid/solid interface. This bottom-up model splits the adsorption process into three reversible phases: biased diffusion, anchoring and lockdown. Statistical analysis highlighted the distinct roles played by regions of the peptide studied here throughout the adsorption process: the hydrophobic domain plays a significant role in the biased diffusion and anchoring phases suggesting that the initial impetus for association between the peptide and the interface may be hydrophobic in origin; aromatic residues dominate the interaction between the peptide and the surface in the adsorbed state and the polar region in the middle of the peptide affords a high conformational flexibility allowing strongly interacting residues to maximise favourable interactions with the surface. Reversible adsorption was observed here, unlike in our prior work focused on a more strongly interacting surface. However, this reversibility is unlikely to be seen once the peptide-surface interaction exceeds 10 kcal mol(-1).
DOI: 10.1039/c5sm00123d
PubMed: 25920450
Affiliations:
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Le document en format XML
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Tamerler</name></author><author><name sortKey="Biggs, M J" sort="Biggs, M J" uniqKey="Biggs M" first="M J" last="Biggs">M J Biggs</name></author></analytic><series><title level="j">Soft matter</title><idno type="eISSN">1744-6848</idno><imprint><date when="2015" type="published">2015</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adsorption (MeSH)</term><term>Diffusion (MeSH)</term><term>Graphite (chemistry)</term><term>Hydrogen Bonding (MeSH)</term><term>Hydrophobic and Hydrophilic Interactions (MeSH)</term><term>Molecular Dynamics Simulation (MeSH)</term><term>Peptides (chemistry)</term><term>Protein Conformation (MeSH)</term><term>Surface Properties (MeSH)</term><term>Thermodynamics (MeSH)</term><term>Water (chemistry)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Adsorption (MeSH)</term><term>Conformation des protéines (MeSH)</term><term>Diffusion (MeSH)</term><term>Eau (composition chimique)</term><term>Graphite (composition chimique)</term><term>Interactions hydrophobes et hydrophiles (MeSH)</term><term>Liaison hydrogène (MeSH)</term><term>Peptides (composition chimique)</term><term>Propriétés de surface (MeSH)</term><term>Simulation de dynamique moléculaire (MeSH)</term><term>Thermodynamique (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Graphite</term><term>Peptides</term><term>Water</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Eau</term><term>Graphite</term><term>Peptides</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Adsorption</term><term>Diffusion</term><term>Hydrogen Bonding</term><term>Hydrophobic and Hydrophilic Interactions</term><term>Molecular Dynamics Simulation</term><term>Protein Conformation</term><term>Surface Properties</term><term>Thermodynamics</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Adsorption</term><term>Conformation des protéines</term><term>Diffusion</term><term>Interactions hydrophobes et hydrophiles</term><term>Liaison hydrogène</term><term>Propriétés de surface</term><term>Simulation de dynamique moléculaire</term><term>Thermodynamique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The association of proteins and peptides with inorganic material has vast technological potential. An understanding of the adsorption of peptides at liquid/solid interfaces on a molecular-level is fundamental to fully realising this potential. Combining our prior work along with the statistical analysis of 100+ molecular dynamics simulations of adsorption of an experimentally identified graphite binding peptide, GrBP5, at the water/graphite interface has been used here to propose a model for the adsorption of a peptide at a liquid/solid interface. This bottom-up model splits the adsorption process into three reversible phases: biased diffusion, anchoring and lockdown. Statistical analysis highlighted the distinct roles played by regions of the peptide studied here throughout the adsorption process: the hydrophobic domain plays a significant role in the biased diffusion and anchoring phases suggesting that the initial impetus for association between the peptide and the interface may be hydrophobic in origin; aromatic residues dominate the interaction between the peptide and the surface in the adsorbed state and the polar region in the middle of the peptide affords a high conformational flexibility allowing strongly interacting residues to maximise favourable interactions with the surface. Reversible adsorption was observed here, unlike in our prior work focused on a more strongly interacting surface. However, this reversibility is unlikely to be seen once the peptide-surface interaction exceeds 10 kcal mol(-1). </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25920450</PMID><DateCompleted><Year>2016</Year><Month>03</Month><Day>22</Day></DateCompleted><DateRevised><Year>2015</Year><Month>06</Month><Day>24</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1744-6848</ISSN><JournalIssue CitedMedium="Internet"><Volume>11</Volume><Issue>26</Issue><PubDate><Year>2015</Year><Month>Jul</Month><Day>14</Day></PubDate></JournalIssue><Title>Soft matter</Title><ISOAbbreviation>Soft Matter</ISOAbbreviation></Journal><ArticleTitle>Molecular-level understanding of the adsorption mechanism of a graphite-binding peptide at the water/graphite interface.</ArticleTitle><Pagination><MedlinePgn>5192-203</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1039/c5sm00123d</ELocationID><Abstract><AbstractText>The association of proteins and peptides with inorganic material has vast technological potential. An understanding of the adsorption of peptides at liquid/solid interfaces on a molecular-level is fundamental to fully realising this potential. Combining our prior work along with the statistical analysis of 100+ molecular dynamics simulations of adsorption of an experimentally identified graphite binding peptide, GrBP5, at the water/graphite interface has been used here to propose a model for the adsorption of a peptide at a liquid/solid interface. This bottom-up model splits the adsorption process into three reversible phases: biased diffusion, anchoring and lockdown. Statistical analysis highlighted the distinct roles played by regions of the peptide studied here throughout the adsorption process: the hydrophobic domain plays a significant role in the biased diffusion and anchoring phases suggesting that the initial impetus for association between the peptide and the interface may be hydrophobic in origin; aromatic residues dominate the interaction between the peptide and the surface in the adsorbed state and the polar region in the middle of the peptide affords a high conformational flexibility allowing strongly interacting residues to maximise favourable interactions with the surface. Reversible adsorption was observed here, unlike in our prior work focused on a more strongly interacting surface. 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Mijajlovic</name><name sortKey="Tamerler, C" sort="Tamerler, C" uniqKey="Tamerler C" first="C" last="Tamerler">C. Tamerler</name></noCountry><country name="Australie"><noRegion><name sortKey="Penna, M J" sort="Penna, M J" uniqKey="Penna M" first="M J" last="Penna">M J Penna</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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