Engineering and functionalization of the disulfide-constrained miniprotein min-23 as a scaffold for diagnostic application.
Identifieur interne : 000E22 ( Main/Exploration ); précédent : 000E21; suivant : 000E23Engineering and functionalization of the disulfide-constrained miniprotein min-23 as a scaffold for diagnostic application.
Auteurs : RBID : pubmed:22213706English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Contrast Media (chemistry), Contrast Media (diagnostic use), Contrast Media (pharmacokinetics), Disulfides (chemistry), Humans, Indium Radioisotopes (chemistry), Isotope Labeling, Mice, Molecular Sequence Data, Neoplasms (radionuclide imaging), Peptides (chemistry), Peptides (diagnostic use), Peptides (pharmacokinetics), Positron-Emission Tomography, Protein Engineering, Protein Folding, Tissue Distribution.
- MESH :
- chemical , chemistry : Contrast Media, Disulfides, Indium Radioisotopes, Peptides.
- chemical , diagnostic use : Contrast Media, Peptides.
- chemical , pharmacokinetics : Contrast Media, Peptides.
- radionuclide imaging : Neoplasms.
- Amino Acid Sequence, Animals, Humans, Isotope Labeling, Mice, Molecular Sequence Data, Positron-Emission Tomography, Protein Engineering, Protein Folding, Tissue Distribution.
Abstract
Miniproteins are scaffolds for the development of alternative non-immunoglobin binding agents for medical applications. This peptide format features high tolerance to sequence mutagenesis, excellent proteolytic stability, and fast blood pool clearance. Herein we present the total chemical synthesis of the disulfide-constrained scaffold Min-23 and its functionalization for in vitro and in vivo application. Optimized solid-phase peptide chemistry and oxidative folding strategies were developed to engineer this miniprotein with native-like disulfide configuration. High levels of serum stability and proteolytic resistance, as well as a beneficial pharmacokinetic profile for diagnostic imaging, were determined by using radiolabeling techniques such as positron emission tomography. The reported achievements highlight Min-23 as a promising scaffold for the development of novel recognition molecules for medical application.
DOI: 10.1002/cmdc.201100497
PubMed: 22213706
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This peptide format features high tolerance to sequence mutagenesis, excellent proteolytic stability, and fast blood pool clearance. Herein we present the total chemical synthesis of the disulfide-constrained scaffold Min-23 and its functionalization for in vitro and in vivo application. Optimized solid-phase peptide chemistry and oxidative folding strategies were developed to engineer this miniprotein with native-like disulfide configuration. High levels of serum stability and proteolytic resistance, as well as a beneficial pharmacokinetic profile for diagnostic imaging, were determined by using radiolabeling techniques such as positron emission tomography. The reported achievements highlight Min-23 as a promising scaffold for the development of novel recognition molecules for medical application.</div></front></TEI><pubmed><MedlineCitation Owner="NLM" Status="MEDLINE"><PMID Version="1">22213706</PMID><DateCreated><Year>2012</Year><Month>01</Month><Day>30</Day></DateCreated><DateCompleted><Year>2012</Year><Month>05</Month><Day>25</Day></DateCompleted><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1860-7187</ISSN><JournalIssue CitedMedium="Internet"><Volume>7</Volume><Issue>2</Issue><PubDate><Year>2012</Year><Month>Feb</Month><Day>6</Day></PubDate></JournalIssue><Title>ChemMedChem</Title><ISOAbbreviation>ChemMedChem</ISOAbbreviation></Journal><ArticleTitle>Engineering and functionalization of the disulfide-constrained miniprotein min-23 as a scaffold for diagnostic application.</ArticleTitle><Pagination><MedlinePgn>237-47</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1002/cmdc.201100497</ELocationID><Abstract><AbstractText>Miniproteins are scaffolds for the development of alternative non-immunoglobin binding agents for medical applications. This peptide format features high tolerance to sequence mutagenesis, excellent proteolytic stability, and fast blood pool clearance. Herein we present the total chemical synthesis of the disulfide-constrained scaffold Min-23 and its functionalization for in vitro and in vivo application. Optimized solid-phase peptide chemistry and oxidative folding strategies were developed to engineer this miniprotein with native-like disulfide configuration. High levels of serum stability and proteolytic resistance, as well as a beneficial pharmacokinetic profile for diagnostic imaging, were determined by using radiolabeling techniques such as positron emission tomography. The reported achievements highlight Min-23 as a promising scaffold for the development of novel recognition molecules for medical application.</AbstractText><CopyrightInformation>Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zoller</LastName><ForeName>Frederic</ForeName><Initials>F</Initials><Affiliation>German Cancer Research Center (DKFZ), Clinical Cooperation Unit Nuclear Medicine, INF 280, 69120 Heidelberg, Germany.</Affiliation></Author><Author ValidYN="Y"><LastName>Schwaebel</LastName><ForeName>Thimon</ForeName><Initials>T</Initials></Author><Author ValidYN="Y"><LastName>Markert</LastName><ForeName>Annette</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Haberkorn</LastName><ForeName>Uwe</ForeName><Initials>U</Initials></Author><Author ValidYN="Y"><LastName>Mier</LastName><ForeName>Walter</ForeName><Initials>W</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType>Journal Article</PublicationType><PublicationType>Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2011</Year><Month>12</Month><Day>23</Day></ArticleDate></Article><MedlineJournalInfo><Country>Germany</Country><MedlineTA>ChemMedChem</MedlineTA><NlmUniqueID>101259013</NlmUniqueID><ISSNLinking>1860-7179</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance>Contrast Media</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance>Disulfides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance>Indium Radioisotopes</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance>Peptides</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Contrast Media</DescriptorName><QualifierName MajorTopicYN="Y">chemistry</QualifierName><QualifierName MajorTopicYN="N">diagnostic use</QualifierName><QualifierName MajorTopicYN="N">pharmacokinetics</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Disulfides</DescriptorName><QualifierName MajorTopicYN="Y">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Indium Radioisotopes</DescriptorName><QualifierName MajorTopicYN="N">chemistry</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Isotope Labeling</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Mice</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Neoplasms</DescriptorName><QualifierName MajorTopicYN="N">radionuclide imaging</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Peptides</DescriptorName><QualifierName MajorTopicYN="Y">chemistry</QualifierName><QualifierName MajorTopicYN="N">diagnostic use</QualifierName><QualifierName MajorTopicYN="N">pharmacokinetics</QualifierName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Positron-Emission Tomography</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Protein Engineering</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Protein Folding</DescriptorName></MeshHeading><MeshHeading><DescriptorName MajorTopicYN="N">Tissue Distribution</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2011</Year><Month>10</Month><Day>26</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2011</Year><Month>11</Month><Day>25</Day></PubMedPubDate><PubMedPubDate PubStatus="aheadofprint"><Year>2011</Year><Month>12</Month><Day>23</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2012</Year><Month>1</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2012</Year><Month>1</Month><Day>4</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2012</Year><Month>5</Month><Day>26</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="doi">10.1002/cmdc.201100497</ArticleId><ArticleId IdType="pubmed">22213706</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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