Protease‐resistant peptide design—empowering nature's fragile warriors against HIV
Identifieur interne : 000347 ( Istex/Checkpoint ); précédent : 000346; suivant : 000348Protease‐resistant peptide design—empowering nature's fragile warriors against HIV
Auteurs : Matthew T. Weinstock [États-Unis] ; J. Nicholas Francis [États-Unis] ; Joseph S. Redman [États-Unis] ; Michael S. Kay [États-Unis]Source :
- Peptide Science [ 0006-3525 ] ; 2012.
English descriptors
- Teeft :
- Acad, Acyclic residues, Amino, Amino acid, Amino acid analogues, Amino acids, Anal biochem, Analogue, Angew, Angew chem, Avidity, Binder, Binding interface, Biol, Biol chem, Biopolymers, Cell receptors, Chem, Chem biol, Chemokine coreceptor, Clinical trials, Codon, Codon reprogramming, Contract grant number, Contract grant sponsor, Control release, Crystal structure, Curr opin chem biol, Cyclic ring acids, Display techniques, Drug discovery, Entry inhibitor, Entry inhibitors, Extensive efforts, Forster, Fuzeon, Genetic code, Hydrophobic pocket, Inhibitor, Inhibitor binding, Library diversity, Ligation, Ligation site, Membrane fusion, Modest potency, Mrna, Natl, Nicholas francis, Peptide, Peptide backbone, Peptide backbones, Peptide design, Peptide fragment, Peptide libraries, Peptide library, Peptide science, Peptide therapeutics, Peptidomimetics, Phage, Phage display, Potency plateau, Proc, Proc natl acad, Protease, Rational design, Recent advances, Repa, Residue, Resistance capacitor, Ribosomal incorporation, Ribosome, Salt lake city, Screen peptide libraries, Selection pressure, Side chains, Small molecule inhibitors, Small molecules, Struct biol, Symmetry relationship, Synthetase pairs, Tetrahedron lett, Therapeutics, Translation system, Trna molecules, Utah school, Viral, Viral entry, Vivo fragility, Wang, Weinstock, Wiley periodicals.
Abstract
Peptides have great potential as therapeutic agents, but their use is often limited by susceptibility to proteolysis and their resulting in vivo fragility. In this review, we focus on peptidomimetic approaches to produce protease‐resistant peptides with the potential for greatly improved clinical utility. We focus on the use of mirror‐image (D‐peptide) and ß‐peptides as two leading approaches with distinct design principles and challenges. Application to the important and difficult problem of inhibiting HIV entry illustrates the current state‐of‐the‐art in peptidomimetic technologies. We also summarize future directions for this field and highlight remaining obstacles to widespread use of protease‐resistant peptides. © 2012 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 98: 431–442, 2012.
Url:
DOI: 10.1002/bip.22073
Affiliations:
Links toward previous steps (curation, corpus...)
Links to Exploration step
ISTEX:A00F12DF0644C0BBBB052EC76AF7E9194F886640Le document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Protease‐resistant peptide design—empowering nature's fragile warriors against HIV</title><author><name sortKey="Weinstock, Matthew T" sort="Weinstock, Matthew T" uniqKey="Weinstock M" first="Matthew T." last="Weinstock">Matthew T. Weinstock</name></author><author><name sortKey="Francis, J Nicholas" sort="Francis, J Nicholas" uniqKey="Francis J" first="J. Nicholas" last="Francis">J. Nicholas Francis</name></author><author><name sortKey="Redman, Joseph S" sort="Redman, Joseph S" uniqKey="Redman J" first="Joseph S." last="Redman">Joseph S. Redman</name></author><author><name sortKey="Kay, Michael S" sort="Kay, Michael S" uniqKey="Kay M" first="Michael S." last="Kay">Michael S. Kay</name></author></titleStmt><publicationStmt><idno type="wicri:source">ISTEX</idno><idno type="RBID">ISTEX:A00F12DF0644C0BBBB052EC76AF7E9194F886640</idno><date when="2012" year="2012">2012</date><idno type="doi">10.1002/bip.22073</idno><idno type="url">https://api.istex.fr/ark:/67375/WNG-DS5J6FPD-X/fulltext.pdf</idno><idno type="wicri:Area/Istex/Corpus">001B85</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">001B85</idno><idno type="wicri:Area/Istex/Curation">001B85</idno><idno type="wicri:Area/Istex/Checkpoint">000347</idno><idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Checkpoint">000347</idno></publicationStmt><sourceDesc><biblStruct><analytic><title level="a" type="main">Protease‐resistant peptide design—empowering nature's fragile warriors against HIV</title><author><name sortKey="Weinstock, Matthew T" sort="Weinstock, Matthew T" uniqKey="Weinstock M" first="Matthew T." last="Weinstock">Matthew T. Weinstock</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Utah</region></placeName><wicri:cityArea>Department of Biochemistry, University of Utah School of Medicine, Salt Lake City</wicri:cityArea></affiliation></author><author><name sortKey="Francis, J Nicholas" sort="Francis, J Nicholas" uniqKey="Francis J" first="J. Nicholas" last="Francis">J. Nicholas Francis</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Utah</region></placeName><wicri:cityArea>Department of Biochemistry, University of Utah School of Medicine, Salt Lake City</wicri:cityArea></affiliation></author><author><name sortKey="Redman, Joseph S" sort="Redman, Joseph S" uniqKey="Redman J" first="Joseph S." last="Redman">Joseph S. Redman</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Utah</region></placeName><wicri:cityArea>Department of Biochemistry, University of Utah School of Medicine, Salt Lake City</wicri:cityArea></affiliation></author><author><name sortKey="Kay, Michael S" sort="Kay, Michael S" uniqKey="Kay M" first="Michael S." last="Kay">Michael S. Kay</name><affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country><placeName><region type="state">Utah</region></placeName><wicri:cityArea>Department of Biochemistry, University of Utah School of Medicine, Salt Lake City</wicri:cityArea></affiliation><affiliation wicri:level="1"><country wicri:rule="url">États-Unis</country></affiliation><affiliation wicri:level="1"><country xml:lang="fr">États-Unis</country><wicri:regionArea>Correspondence address: Department of Biochemistry, University of Utah School of Medicine, 15 N Medical Drive East Rm 4100, Salt Lake City, UT 84112‐5650</wicri:regionArea><wicri:noRegion>UT 84112‐5650</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Peptide Science</title><title level="j" type="alt">PEPTIDE SCIENCE</title><idno type="ISSN">0006-3525</idno><idno type="eISSN">1097-0282</idno><imprint><biblScope unit="vol">98</biblScope><biblScope unit="issue">5</biblScope><biblScope unit="page" from="431">431</biblScope><biblScope unit="page" to="442">442</biblScope><biblScope unit="page-count">12</biblScope><publisher>Wiley Subscription Services, Inc., A Wiley Company</publisher><pubPlace>Hoboken</pubPlace><date type="published" when="2012">2012</date></imprint><idno type="ISSN">0006-3525</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0006-3525</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Acad</term><term>Acyclic residues</term><term>Amino</term><term>Amino acid</term><term>Amino acid analogues</term><term>Amino acids</term><term>Anal biochem</term><term>Analogue</term><term>Angew</term><term>Angew chem</term><term>Avidity</term><term>Binder</term><term>Binding interface</term><term>Biol</term><term>Biol chem</term><term>Biopolymers</term><term>Cell receptors</term><term>Chem</term><term>Chem biol</term><term>Chemokine coreceptor</term><term>Clinical trials</term><term>Codon</term><term>Codon reprogramming</term><term>Contract grant number</term><term>Contract grant sponsor</term><term>Control release</term><term>Crystal structure</term><term>Curr opin chem biol</term><term>Cyclic ring acids</term><term>Display techniques</term><term>Drug discovery</term><term>Entry inhibitor</term><term>Entry inhibitors</term><term>Extensive efforts</term><term>Forster</term><term>Fuzeon</term><term>Genetic code</term><term>Hydrophobic pocket</term><term>Inhibitor</term><term>Inhibitor binding</term><term>Library diversity</term><term>Ligation</term><term>Ligation site</term><term>Membrane fusion</term><term>Modest potency</term><term>Mrna</term><term>Natl</term><term>Nicholas francis</term><term>Peptide</term><term>Peptide backbone</term><term>Peptide backbones</term><term>Peptide design</term><term>Peptide fragment</term><term>Peptide libraries</term><term>Peptide library</term><term>Peptide science</term><term>Peptide therapeutics</term><term>Peptidomimetics</term><term>Phage</term><term>Phage display</term><term>Potency plateau</term><term>Proc</term><term>Proc natl acad</term><term>Protease</term><term>Rational design</term><term>Recent advances</term><term>Repa</term><term>Residue</term><term>Resistance capacitor</term><term>Ribosomal incorporation</term><term>Ribosome</term><term>Salt lake city</term><term>Screen peptide libraries</term><term>Selection pressure</term><term>Side chains</term><term>Small molecule inhibitors</term><term>Small molecules</term><term>Struct biol</term><term>Symmetry relationship</term><term>Synthetase pairs</term><term>Tetrahedron lett</term><term>Therapeutics</term><term>Translation system</term><term>Trna molecules</term><term>Utah school</term><term>Viral</term><term>Viral entry</term><term>Vivo fragility</term><term>Wang</term><term>Weinstock</term><term>Wiley periodicals</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Peptides have great potential as therapeutic agents, but their use is often limited by susceptibility to proteolysis and their resulting in vivo fragility. In this review, we focus on peptidomimetic approaches to produce protease‐resistant peptides with the potential for greatly improved clinical utility. We focus on the use of mirror‐image (D‐peptide) and ß‐peptides as two leading approaches with distinct design principles and challenges. Application to the important and difficult problem of inhibiting HIV entry illustrates the current state‐of‐the‐art in peptidomimetic technologies. We also summarize future directions for this field and highlight remaining obstacles to widespread use of protease‐resistant peptides. © 2012 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 98: 431–442, 2012.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Utah</li></region></list><tree><country name="États-Unis"><region name="Utah"><name sortKey="Weinstock, Matthew T" sort="Weinstock, Matthew T" uniqKey="Weinstock M" first="Matthew T." last="Weinstock">Matthew T. Weinstock</name></region><name sortKey="Francis, J Nicholas" sort="Francis, J Nicholas" uniqKey="Francis J" first="J. Nicholas" last="Francis">J. Nicholas Francis</name><name sortKey="Kay, Michael S" sort="Kay, Michael S" uniqKey="Kay M" first="Michael S." last="Kay">Michael S. Kay</name><name sortKey="Kay, Michael S" sort="Kay, Michael S" uniqKey="Kay M" first="Michael S." last="Kay">Michael S. Kay</name><name sortKey="Kay, Michael S" sort="Kay, Michael S" uniqKey="Kay M" first="Michael S." last="Kay">Michael S. Kay</name><name sortKey="Redman, Joseph S" sort="Redman, Joseph S" uniqKey="Redman J" first="Joseph S." last="Redman">Joseph S. Redman</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/MersV1/Data/Istex/Checkpoint
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000347 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Istex/Checkpoint/biblio.hfd -nk 000347 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= MersV1
|flux= Istex
|étape= Checkpoint
|type= RBID
|clé= ISTEX:A00F12DF0644C0BBBB052EC76AF7E9194F886640
|texte= Protease‐resistant peptide design—empowering nature's fragile warriors against HIV
}}
| This area was generated with Dilib version V0.6.33. |  |