Investigation of self-assembling proline- and glycine-rich recombinant proteins and peptides inspired by proteins from a symbiotic fungus using atomic force microscopy and circular dichroism spectroscopy.
Identifieur interne : 002038 ( Main/Corpus ); précédent : 002037; suivant : 002039Investigation of self-assembling proline- and glycine-rich recombinant proteins and peptides inspired by proteins from a symbiotic fungus using atomic force microscopy and circular dichroism spectroscopy.
Auteurs : Rhiannon G. Creasey ; Nicolas H. Voelcker ; Carolyn J. SchultzSource :
- Biochimica et biophysica acta [ 0006-3002 ] ; 2012.
English descriptors
- KwdEn :
- Biomimetic Materials (chemical synthesis), Circular Dichroism (MeSH), Escherichia coli (genetics), Microscopy, Atomic Force (MeSH), Microscopy, Electron, Scanning (MeSH), Mucoproteins (biosynthesis), Mucoproteins (chemistry), Mucoproteins (genetics), Mycorrhizae (chemistry), Mycorrhizae (physiology), Nanofibers (chemistry), Nanofibers (ultrastructure), Osmolar Concentration (MeSH), Peptides (chemical synthesis), Peptides (chemistry), Plant Proteins (biosynthesis), Plant Proteins (chemistry), Plant Proteins (genetics), Plants (microbiology), Point Mutation (MeSH), Polylysine (chemistry), Protein Structure, Secondary (MeSH), Recombinant Proteins (biosynthesis), Recombinant Proteins (chemistry), Recombinant Proteins (genetics), Symbiosis (MeSH).
- MESH :
- chemical , biosynthesis : Mucoproteins, Plant Proteins, Recombinant Proteins.
- chemical synthesis : Biomimetic Materials, Peptides.
- chemical , chemistry : Mucoproteins, Mycorrhizae, Nanofibers, Peptides, Plant Proteins, Polylysine, Recombinant Proteins.
- genetics : Escherichia coli, Mucoproteins, Plant Proteins, Recombinant Proteins.
- microbiology : Plants.
- physiology : Mycorrhizae.
- ultrastructure : Nanofibers.
- Circular Dichroism, Microscopy, Atomic Force, Microscopy, Electron, Scanning, Osmolar Concentration, Point Mutation, Protein Structure, Secondary, Symbiosis.
Abstract
Fiber-forming proteins and peptides are being scrutinized as a promising source of building blocks for new nanomaterials. Arabinogalactan-like (AGL) proteins expressed at the symbiotic interface between plant roots and arbuscular mycorrhizal fungi have novel sequences, hypothesized to form polyproline II (PPII) helix structures. The functional nature of these proteins is unknown but they may form structures for the establishment and maintenance of fungal hyphae. Here we show that recombinant AGL1 (rAGL1) and recombinant AGL3 (rAGL3) are extended proteins based upon secondary structural characteristics determined by electronic circular dichroism (CD) spectroscopy and can self-assemble into fibers and microtubes as observed by atomic force microscopy (AFM) and scanning electron microscopy (SEM). CD spectroscopy results of synthetic peptides based on repeat regions in AGL1, AGL2 and AGL3 suggest that the synthetic peptides contain significant amounts of extended PPII helices and that these structures are influenced by ionic strength and, at least in one case, by concentration. Point mutations of a single residue of the repeat region of AGL3 resulted in altered secondary structures. Self-assembly of these repeats was observed by means of AFM and optical microscopy. Peptide (APADGK)(6) forms structures with similar morphology to rAGL1 suggesting that these repeats are crucial for the morphology of rAGL1 fibers. These novel self-assembling sequences may find applications as precursors for bioinspired nanomaterials.
DOI: 10.1016/j.bbapap.2012.02.009
PubMed: 22425601
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Investigation of self-assembling proline- and glycine-rich recombinant proteins and peptides inspired by proteins from a symbiotic fungus using atomic force microscopy and circular dichroism spectroscopy.</title><author><name sortKey="Creasey, Rhiannon G" sort="Creasey, Rhiannon G" uniqKey="Creasey R" first="Rhiannon G" last="Creasey">Rhiannon G. Creasey</name><affiliation><nlm:affiliation>School of Chemical and Physical Sciences, Flinders University of South Australia, Australia. rhiannon.creasey@flinders.edu.au</nlm:affiliation></affiliation></author><author><name sortKey="Voelcker, Nicolas H" sort="Voelcker, Nicolas H" uniqKey="Voelcker N" first="Nicolas H" last="Voelcker">Nicolas H. Voelcker</name></author><author><name sortKey="Schultz, Carolyn J" sort="Schultz, Carolyn J" uniqKey="Schultz C" first="Carolyn J" last="Schultz">Carolyn J. Schultz</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2012">2012</date><idno type="RBID">pubmed:22425601</idno><idno type="pmid">22425601</idno><idno type="doi">10.1016/j.bbapap.2012.02.009</idno><idno type="wicri:Area/Main/Corpus">002038</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">002038</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Investigation of self-assembling proline- and glycine-rich recombinant proteins and peptides inspired by proteins from a symbiotic fungus using atomic force microscopy and circular dichroism spectroscopy.</title><author><name sortKey="Creasey, Rhiannon G" sort="Creasey, Rhiannon G" uniqKey="Creasey R" first="Rhiannon G" last="Creasey">Rhiannon G. Creasey</name><affiliation><nlm:affiliation>School of Chemical and Physical Sciences, Flinders University of South Australia, Australia. rhiannon.creasey@flinders.edu.au</nlm:affiliation></affiliation></author><author><name sortKey="Voelcker, Nicolas H" sort="Voelcker, Nicolas H" uniqKey="Voelcker N" first="Nicolas H" last="Voelcker">Nicolas H. Voelcker</name></author><author><name sortKey="Schultz, Carolyn J" sort="Schultz, Carolyn J" uniqKey="Schultz C" first="Carolyn J" last="Schultz">Carolyn J. Schultz</name></author></analytic><series><title level="j">Biochimica et biophysica acta</title><idno type="ISSN">0006-3002</idno><imprint><date when="2012" type="published">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Biomimetic Materials (chemical synthesis)</term><term>Circular Dichroism (MeSH)</term><term>Escherichia coli (genetics)</term><term>Microscopy, Atomic Force (MeSH)</term><term>Microscopy, Electron, Scanning (MeSH)</term><term>Mucoproteins (biosynthesis)</term><term>Mucoproteins (chemistry)</term><term>Mucoproteins (genetics)</term><term>Mycorrhizae (chemistry)</term><term>Mycorrhizae (physiology)</term><term>Nanofibers (chemistry)</term><term>Nanofibers (ultrastructure)</term><term>Osmolar Concentration (MeSH)</term><term>Peptides (chemical synthesis)</term><term>Peptides (chemistry)</term><term>Plant Proteins (biosynthesis)</term><term>Plant Proteins (chemistry)</term><term>Plant Proteins (genetics)</term><term>Plants (microbiology)</term><term>Point Mutation (MeSH)</term><term>Polylysine (chemistry)</term><term>Protein Structure, Secondary (MeSH)</term><term>Recombinant Proteins (biosynthesis)</term><term>Recombinant Proteins (chemistry)</term><term>Recombinant Proteins (genetics)</term><term>Symbiosis (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Mucoproteins</term><term>Plant Proteins</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="chemical synthesis" xml:lang="en"><term>Biomimetic Materials</term><term>Peptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Mucoproteins</term><term>Mycorrhizae</term><term>Nanofibers</term><term>Peptides</term><term>Plant Proteins</term><term>Polylysine</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Escherichia coli</term><term>Mucoproteins</term><term>Plant Proteins</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" qualifier="microbiology" xml:lang="en"><term>Plants</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Mycorrhizae</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="en"><term>Nanofibers</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Circular Dichroism</term><term>Microscopy, Atomic Force</term><term>Microscopy, Electron, Scanning</term><term>Osmolar Concentration</term><term>Point Mutation</term><term>Protein Structure, Secondary</term><term>Symbiosis</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Fiber-forming proteins and peptides are being scrutinized as a promising source of building blocks for new nanomaterials. Arabinogalactan-like (AGL) proteins expressed at the symbiotic interface between plant roots and arbuscular mycorrhizal fungi have novel sequences, hypothesized to form polyproline II (PPII) helix structures. The functional nature of these proteins is unknown but they may form structures for the establishment and maintenance of fungal hyphae. Here we show that recombinant AGL1 (rAGL1) and recombinant AGL3 (rAGL3) are extended proteins based upon secondary structural characteristics determined by electronic circular dichroism (CD) spectroscopy and can self-assemble into fibers and microtubes as observed by atomic force microscopy (AFM) and scanning electron microscopy (SEM). CD spectroscopy results of synthetic peptides based on repeat regions in AGL1, AGL2 and AGL3 suggest that the synthetic peptides contain significant amounts of extended PPII helices and that these structures are influenced by ionic strength and, at least in one case, by concentration. Point mutations of a single residue of the repeat region of AGL3 resulted in altered secondary structures. Self-assembly of these repeats was observed by means of AFM and optical microscopy. Peptide (APADGK)(6) forms structures with similar morphology to rAGL1 suggesting that these repeats are crucial for the morphology of rAGL1 fibers. These novel self-assembling sequences may find applications as precursors for bioinspired nanomaterials.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22425601</PMID><DateCompleted><Year>2013</Year><Month>04</Month><Day>02</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>26</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">0006-3002</ISSN><JournalIssue CitedMedium="Print"><Volume>1824</Volume><Issue>5</Issue><PubDate><Year>2012</Year><Month>May</Month></PubDate></JournalIssue><Title>Biochimica et biophysica acta</Title><ISOAbbreviation>Biochim Biophys Acta</ISOAbbreviation></Journal><ArticleTitle>Investigation of self-assembling proline- and glycine-rich recombinant proteins and peptides inspired by proteins from a symbiotic fungus using atomic force microscopy and circular dichroism spectroscopy.</ArticleTitle><Pagination><MedlinePgn>711-22</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbapap.2012.02.009</ELocationID><Abstract><AbstractText>Fiber-forming proteins and peptides are being scrutinized as a promising source of building blocks for new nanomaterials. Arabinogalactan-like (AGL) proteins expressed at the symbiotic interface between plant roots and arbuscular mycorrhizal fungi have novel sequences, hypothesized to form polyproline II (PPII) helix structures. The functional nature of these proteins is unknown but they may form structures for the establishment and maintenance of fungal hyphae. Here we show that recombinant AGL1 (rAGL1) and recombinant AGL3 (rAGL3) are extended proteins based upon secondary structural characteristics determined by electronic circular dichroism (CD) spectroscopy and can self-assemble into fibers and microtubes as observed by atomic force microscopy (AFM) and scanning electron microscopy (SEM). CD spectroscopy results of synthetic peptides based on repeat regions in AGL1, AGL2 and AGL3 suggest that the synthetic peptides contain significant amounts of extended PPII helices and that these structures are influenced by ionic strength and, at least in one case, by concentration. Point mutations of a single residue of the repeat region of AGL3 resulted in altered secondary structures. Self-assembly of these repeats was observed by means of AFM and optical microscopy. Peptide (APADGK)(6) forms structures with similar morphology to rAGL1 suggesting that these repeats are crucial for the morphology of rAGL1 fibers. These novel self-assembling sequences may find applications as precursors for bioinspired nanomaterials.</AbstractText><CopyrightInformation>Copyright © 2012 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Creasey</LastName><ForeName>Rhiannon G</ForeName><Initials>RG</Initials><AffiliationInfo><Affiliation>School of Chemical and Physical Sciences, Flinders University of South Australia, Australia. rhiannon.creasey@flinders.edu.au</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Voelcker</LastName><ForeName>Nicolas H</ForeName><Initials>NH</Initials></Author><Author ValidYN="Y"><LastName>Schultz</LastName><ForeName>Carolyn J</ForeName><Initials>CJ</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2012</Year><Month>03</Month><Day>03</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biochim Biophys 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