Thrombogenic collagen-mimetic peptides: Self-assembly of triple helix-based fibrils driven by hydrophobic interactions.
Identifieur interne : 002100 ( PubMed/Curation ); précédent : 002099; suivant : 002101Thrombogenic collagen-mimetic peptides: Self-assembly of triple helix-based fibrils driven by hydrophobic interactions.
Auteurs : Mabel A. Cejas [États-Unis] ; William A. Kinney ; Cailin Chen ; Jeremy G. Vinter ; Harold R. Almond ; Karin M. Balss ; Cynthia A. Maryanoff ; Ute Schmidt ; Michael Breslav ; Andrew Mahan ; Eilyn Lacy ; Bruce E. MaryanoffSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 1091-6490 ] ; 2008.
Descripteurs français
- KwdFr :
- MESH :
- métabolisme : Collagènes fibrillaires, Thrombine.
- synthèse chimique : Peptides.
- Biomimétique, Collagènes fibrillaires, Dichroïsme circulaire, Humains, Interactions hydrophobes et hydrophiles, Microscopie à force atomique, Modèles moléculaires, Peptides, Thrombine.
English descriptors
- KwdEn :
- MESH :
- chemical , chemical synthesis : Peptides.
- chemical , chemistry : Fibrillar Collagens, Peptides, Thrombin.
- chemical , metabolism : Fibrillar Collagens, Thrombin.
- Biomimetics, Circular Dichroism, Humans, Hydrophobic and Hydrophilic Interactions, Microscopy, Atomic Force, Models, Molecular.
Abstract
Collagens are integral structural proteins in animal tissues and play key functional roles in cellular modulation. We sought to discover collagen model peptides (CMPs) that would form triple helices and self-assemble into supramolecular fibrils exhibiting collagen-like biological activity without preorganizing the peptide chains by covalent linkages. This challenging objective was accomplished by placing aromatic groups on the ends of a representative 30-mer CMP, (GPO)(10), as with l-phenylalanine and l-pentafluorophenylalanine in 32-mer 1a. Computational studies on homologous 29-mers 1a'-d' (one less GPO), as pairs of triple helices interacting head-to-tail, yielded stabilization energies in the order 1a' > 1b' > 1c' > 1d', supporting the hypothesis that hydrophobic aromatic groups can drive CMP self-assembly. Peptides 1a-d were studied comparatively relative to structural properties and ability to stimulate human platelets. Although each 32-mer formed stable triple helices (CD) spectroscopy, only 1a and 1b self-assembled into micrometer-scale fibrils. Light microscopy images for 1a depicted long collagen-like fibrils, whereas images for 1d did not. Atomic force microscopy topographical images indicated that 1a and 1b self-organize into microfibrillar species, whereas 1c and 1d do not. Peptides 1a and 1b induced the aggregation of human blood platelets with a potency similar to type I collagen, whereas 1c was much less effective, and 1d was inactive (EC(50) potency: 1a/1b > 1c > 1d). Thus, 1a and 1b spontaneously self-assemble into thrombogenic collagen-mimetic materials because of hydrophobic aromatic interactions provided by the special end-groups. These findings have important implications for the design of biofunctional CMPs.
DOI: 10.1073/pnas.0800291105
PubMed: 18559857
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Maryanoff</name></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="eISSN">1091-6490</idno><imprint><date when="2008" type="published">2008</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Biomimetics</term><term>Circular Dichroism</term><term>Fibrillar Collagens (chemistry)</term><term>Fibrillar Collagens (metabolism)</term><term>Humans</term><term>Hydrophobic and Hydrophilic Interactions</term><term>Microscopy, Atomic Force</term><term>Models, Molecular</term><term>Peptides (chemical synthesis)</term><term>Peptides (chemistry)</term><term>Thrombin (chemistry)</term><term>Thrombin (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Biomimétique</term><term>Collagènes fibrillaires ()</term><term>Collagènes fibrillaires (métabolisme)</term><term>Dichroïsme circulaire</term><term>Humains</term><term>Interactions hydrophobes et hydrophiles</term><term>Microscopie à force atomique</term><term>Modèles moléculaires</term><term>Peptides ()</term><term>Peptides (synthèse chimique)</term><term>Thrombine ()</term><term>Thrombine (métabolisme)</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>Fibrillar Collagens</term><term>Peptides</term><term>Thrombin</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Fibrillar Collagens</term><term>Thrombin</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Collagènes fibrillaires</term><term>Thrombine</term></keywords><keywords scheme="MESH" qualifier="synthèse chimique" xml:lang="fr"><term>Peptides</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Biomimetics</term><term>Circular Dichroism</term><term>Humans</term><term>Hydrophobic and Hydrophilic Interactions</term><term>Microscopy, Atomic Force</term><term>Models, Molecular</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Biomimétique</term><term>Collagènes fibrillaires</term><term>Dichroïsme circulaire</term><term>Humains</term><term>Interactions hydrophobes et hydrophiles</term><term>Microscopie à force atomique</term><term>Modèles moléculaires</term><term>Peptides</term><term>Thrombine</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Collagens are integral structural proteins in animal tissues and play key functional roles in cellular modulation. We sought to discover collagen model peptides (CMPs) that would form triple helices and self-assemble into supramolecular fibrils exhibiting collagen-like biological activity without preorganizing the peptide chains by covalent linkages. This challenging objective was accomplished by placing aromatic groups on the ends of a representative 30-mer CMP, (GPO)(10), as with l-phenylalanine and l-pentafluorophenylalanine in 32-mer 1a. Computational studies on homologous 29-mers 1a'-d' (one less GPO), as pairs of triple helices interacting head-to-tail, yielded stabilization energies in the order 1a' > 1b' > 1c' > 1d', supporting the hypothesis that hydrophobic aromatic groups can drive CMP self-assembly. Peptides 1a-d were studied comparatively relative to structural properties and ability to stimulate human platelets. Although each 32-mer formed stable triple helices (CD) spectroscopy, only 1a and 1b self-assembled into micrometer-scale fibrils. Light microscopy images for 1a depicted long collagen-like fibrils, whereas images for 1d did not. Atomic force microscopy topographical images indicated that 1a and 1b self-organize into microfibrillar species, whereas 1c and 1d do not. Peptides 1a and 1b induced the aggregation of human blood platelets with a potency similar to type I collagen, whereas 1c was much less effective, and 1d was inactive (EC(50) potency: 1a/1b > 1c > 1d). Thus, 1a and 1b spontaneously self-assemble into thrombogenic collagen-mimetic materials because of hydrophobic aromatic interactions provided by the special end-groups. These findings have important implications for the design of biofunctional CMPs.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18559857</PMID><DateCompleted><Year>2008</Year><Month>08</Month><Day>19</Day></DateCompleted><DateRevised><Year>2018</Year><Month>12</Month><Day>27</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1091-6490</ISSN><JournalIssue CitedMedium="Internet"><Volume>105</Volume><Issue>25</Issue><PubDate><Year>2008</Year><Month>Jun</Month><Day>24</Day></PubDate></JournalIssue><Title>Proceedings of the National Academy of Sciences of the United States of America</Title><ISOAbbreviation>Proc. Natl. Acad. Sci. U.S.A.</ISOAbbreviation></Journal><ArticleTitle>Thrombogenic collagen-mimetic peptides: Self-assembly of triple helix-based fibrils driven by hydrophobic interactions.</ArticleTitle><Pagination><MedlinePgn>8513-8</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1073/pnas.0800291105</ELocationID><Abstract><AbstractText>Collagens are integral structural proteins in animal tissues and play key functional roles in cellular modulation. We sought to discover collagen model peptides (CMPs) that would form triple helices and self-assemble into supramolecular fibrils exhibiting collagen-like biological activity without preorganizing the peptide chains by covalent linkages. This challenging objective was accomplished by placing aromatic groups on the ends of a representative 30-mer CMP, (GPO)(10), as with l-phenylalanine and l-pentafluorophenylalanine in 32-mer 1a. Computational studies on homologous 29-mers 1a'-d' (one less GPO), as pairs of triple helices interacting head-to-tail, yielded stabilization energies in the order 1a' > 1b' > 1c' > 1d', supporting the hypothesis that hydrophobic aromatic groups can drive CMP self-assembly. Peptides 1a-d were studied comparatively relative to structural properties and ability to stimulate human platelets. Although each 32-mer formed stable triple helices (CD) spectroscopy, only 1a and 1b self-assembled into micrometer-scale fibrils. Light microscopy images for 1a depicted long collagen-like fibrils, whereas images for 1d did not. Atomic force microscopy topographical images indicated that 1a and 1b self-organize into microfibrillar species, whereas 1c and 1d do not. Peptides 1a and 1b induced the aggregation of human blood platelets with a potency similar to type I collagen, whereas 1c was much less effective, and 1d was inactive (EC(50) potency: 1a/1b > 1c > 1d). Thus, 1a and 1b spontaneously self-assemble into thrombogenic collagen-mimetic materials because of hydrophobic aromatic interactions provided by the special end-groups. These findings have important implications for the design of biofunctional CMPs.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Cejas</LastName><ForeName>Mabel A</ForeName><Initials>MA</Initials><AffiliationInfo><Affiliation>Research and Early Development, Johnson & Johnson Pharmaceutical Research & Development, Spring House, PA 19477-0776, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kinney</LastName><ForeName>William A</ForeName><Initials>WA</Initials></Author><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Cailin</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Vinter</LastName><ForeName>Jeremy G</ForeName><Initials>JG</Initials></Author><Author ValidYN="Y"><LastName>Almond</LastName><ForeName>Harold R</ForeName><Initials>HR</Initials><Suffix>Jr</Suffix></Author><Author ValidYN="Y"><LastName>Balss</LastName><ForeName>Karin M</ForeName><Initials>KM</Initials></Author><Author ValidYN="Y"><LastName>Maryanoff</LastName><ForeName>Cynthia A</ForeName><Initials>CA</Initials></Author><Author ValidYN="Y"><LastName>Schmidt</LastName><ForeName>Ute</ForeName><Initials>U</Initials></Author><Author ValidYN="Y"><LastName>Breslav</LastName><ForeName>Michael</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Mahan</LastName><ForeName>Andrew</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Lacy</LastName><ForeName>Eilyn</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Maryanoff</LastName><ForeName>Bruce E</ForeName><Initials>BE</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2008</Year><Month>06</Month><Day>16</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Proc Natl Acad Sci U S A</MedlineTA><NlmUniqueID>7505876</NlmUniqueID><ISSNLinking>0027-8424</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D024022">Fibrillar Collagens</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010455">Peptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.21.5</RegistryNumber><NameOfSubstance UI="D013917">Thrombin</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D032701" MajorTopicYN="N">Biomimetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002942" MajorTopicYN="N">Circular Dichroism</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D024022" MajorTopicYN="N">Fibrillar Collagens</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D057927" MajorTopicYN="N">Hydrophobic and Hydrophilic Interactions</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D018625" MajorTopicYN="N">Microscopy, Atomic Force</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010455" MajorTopicYN="N">Peptides</DescriptorName><QualifierName UI="Q000138" MajorTopicYN="N">chemical synthesis</QualifierName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013917" MajorTopicYN="N">Thrombin</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" 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|texte= Thrombogenic collagen-mimetic peptides: Self-assembly of triple helix-based fibrils driven by hydrophobic interactions.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Curation/RBID.i -Sk "pubmed:18559857" \
| HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Curation/biblio.hfd \
| NlmPubMed2Wicri -a MersV1
| This area was generated with Dilib version V0.6.33. |  |