Differential Effects of β3 - versus β2 -Amino Acid Residues on the Helicity and Recognition Properties of Bim BH3-Derived α/β-Peptides.
Identifieur interne : 000A04 ( Main/Exploration ); précédent : 000A03; suivant : 000A05Differential Effects of β3 - versus β2 -Amino Acid Residues on the Helicity and Recognition Properties of Bim BH3-Derived α/β-Peptides.
Auteurs : Geoffrey A. Eddinger [États-Unis] ; Samuel H. Gellman [États-Unis]Source :
- Angewandte Chemie (International ed. in English) [ 1521-3773 ] ; 2018.
Descripteurs français
- KwdFr :
- MESH :
English descriptors
- KwdEn :
- MESH :
- chemical , chemistry : Amino Acids, Peptides.
- chemical , metabolism : Apoptosis Regulatory Proteins.
- Amino Acid Sequence, Circular Dichroism, Protein Interaction Domains and Motifs, Protein Structure, Secondary, Spectrophotometry, Ultraviolet.
Abstract
Oligomers containing α- and β-amino acid residues (α/β-peptides) have been shown to mimic the α-helical conformation of conventional peptides when the unnatural residues are derived from β3 -amino acids or cyclic β-amino acids, but the impact of incorporating β2 residues has received little attention. The effects of β2 residues on the conformation and recognition behavior of α/β-peptides that mimic an isolated α-helix were investigated. This effort has focused on 26-mers based on the Bim BH3 domain; a set of isomers with identical α/β backbones that differ only in the placement of certain side chains along the backbone (β3 vs. β2 substitution) was compared. Circular dichroism data suggest that β2 residues can be helix-destabilizing relative to β3 residues, although the size of this effect seems to depend on side chain identity. Binding data show that β3 →β2 substitution at sites that contact a partner protein, Bcl-xL , can influence affinity in a way that transcends effects on helicity.
DOI: 10.1002/anie.201806909
PubMed: 30161284
Affiliations:
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Eddinger</name><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, WI, 53706, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, WI, 53706</wicri:regionArea><wicri:noRegion>53706</wicri:noRegion></affiliation></author><author><name sortKey="Gellman, Samuel H" sort="Gellman, Samuel H" uniqKey="Gellman S" first="Samuel H" last="Gellman">Samuel H. Gellman</name><affiliation wicri:level="1"><nlm:affiliation>Department of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, WI, 53706, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, WI, 53706</wicri:regionArea><wicri:noRegion>53706</wicri:noRegion></affiliation></author></analytic><series><title level="j">Angewandte Chemie (International ed. in English)</title><idno type="eISSN">1521-3773</idno><imprint><date when="2018" type="published">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Amino Acids (chemistry)</term><term>Apoptosis Regulatory Proteins (metabolism)</term><term>Circular Dichroism</term><term>Peptides (chemistry)</term><term>Protein Interaction Domains and Motifs</term><term>Protein Structure, Secondary</term><term>Spectrophotometry, Ultraviolet</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Acides aminés ()</term><term>Dichroïsme circulaire</term><term>Motifs et domaines d'intéraction protéique</term><term>Peptides ()</term><term>Protéines régulatrices de l'apoptose (métabolisme)</term><term>Spectrophotométrie UV</term><term>Structure secondaire des protéines</term><term>Séquence d'acides aminés</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Amino Acids</term><term>Peptides</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Apoptosis Regulatory Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéines régulatrices de l'apoptose</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Circular Dichroism</term><term>Protein Interaction Domains and Motifs</term><term>Protein Structure, Secondary</term><term>Spectrophotometry, Ultraviolet</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Acides aminés</term><term>Dichroïsme circulaire</term><term>Motifs et domaines d'intéraction protéique</term><term>Peptides</term><term>Spectrophotométrie UV</term><term>Structure secondaire des protéines</term><term>Séquence d'acides aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Oligomers containing α- and β-amino acid residues (α/β-peptides) have been shown to mimic the α-helical conformation of conventional peptides when the unnatural residues are derived from β<sup>3</sup> -amino acids or cyclic β-amino acids, but the impact of incorporating β<sup>2</sup> residues has received little attention. The effects of β<sup>2</sup> residues on the conformation and recognition behavior of α/β-peptides that mimic an isolated α-helix were investigated. This effort has focused on 26-mers based on the Bim BH3 domain; a set of isomers with identical α/β backbones that differ only in the placement of certain side chains along the backbone (β<sup>3</sup> vs. β<sup>2</sup> substitution) was compared. Circular dichroism data suggest that β<sup>2</sup> residues can be helix-destabilizing relative to β<sup>3</sup> residues, although the size of this effect seems to depend on side chain identity. Binding data show that β<sup>3</sup> →β<sup>2</sup> substitution at sites that contact a partner protein, Bcl-x<sub>L</sub> , can influence affinity in a way that transcends effects on helicity.</div></front></TEI><affiliations><list><country><li>États-Unis</li></country></list><tree><country name="États-Unis"><noRegion><name sortKey="Eddinger, Geoffrey A" sort="Eddinger, Geoffrey A" uniqKey="Eddinger G" first="Geoffrey A" last="Eddinger">Geoffrey A. Eddinger</name></noRegion><name sortKey="Gellman, Samuel H" sort="Gellman, Samuel H" uniqKey="Gellman S" first="Samuel H" last="Gellman">Samuel H. Gellman</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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