MersV1, PubMed, Corpus, bibRecord, 000792

Differential Effects of β3 - versus β2 -Amino Acid Residues on the Helicity and Recognition Properties of Bim BH3-Derived α/β-Peptides.

Identifieur interne : 000792 ( PubMed/Corpus ); précédent : 000791; suivant : 000793

Differential 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 ; Samuel H. Gellman

Source :

Angewandte Chemie (International ed. in English) [ 1521-3773 ] ; 2018.

RBID : pubmed:30161284

English descriptors

KwdEn :
- Amino Acid Sequence, Amino Acids (chemistry), Apoptosis Regulatory Proteins (metabolism), Circular Dichroism, Peptides (chemistry), Protein Interaction Domains and Motifs, Protein Structure, Secondary, Spectrophotometry, Ultraviolet.
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-x_L , can influence affinity in a way that transcends effects on helicity.

DOI: 10.1002/anie.201806909
PubMed: 30161284

Links to Exploration step

pubmed:30161284

Le document en format XML

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 - versus β<sup>2</sup>
 -Amino Acid Residues on the Helicity and Recognition Properties of Bim BH3-Derived α/β-Peptides.</title>
<author><name sortKey="Eddinger, Geoffrey A" sort="Eddinger, Geoffrey A" uniqKey="Eddinger G" first="Geoffrey A" last="Eddinger">Geoffrey A. Eddinger</name>
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<author><name sortKey="Gellman, Samuel H" sort="Gellman, Samuel H" uniqKey="Gellman S" first="Samuel H" last="Gellman">Samuel H. Gellman</name>
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<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>
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 - versus β<sup>2</sup>
 -Amino Acid Residues on the Helicity and Recognition Properties of Bim BH3-Derived α/β-Peptides.</ArticleTitle>
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<Abstract><AbstractText>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.</AbstractText>
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   |clé=     pubmed:30161284
   |texte=   Differential Effects of β3 - versus β2 -Amino Acid Residues on the Helicity and Recognition Properties of Bim BH3-Derived α/β-Peptides.
}}

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Differential Effects of β3 - versus β2 -Amino Acid Residues on the Helicity and Recognition Properties of Bim BH3-Derived α/β-Peptides.

Differential Effects of β3 - versus β2 -Amino Acid Residues on the Helicity and Recognition Properties of Bim BH3-Derived α/β-Peptides.

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