Bis-Lactam Peptide [ i , i +4]-Stapling with α-Methylated Thialysines

Four bis-lactam [ , +4]-stapled peptides with d- or l-α-methyl-thialysines were constructed on a model peptide sequence derived from p110α[E545K] and subjected to circular dichroism (CD) and proteolytic stability assessment, alongside the corresponding bis-lactam [ , +4]-stapled peptide with l-thial...

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Veröffentlicht in:Molecules (Basel, Switzerland) Switzerland), 2020-10, Vol.25 (19), p.4506
Hauptverfasser: Wu, Bo, Zheng, Weiping
Format: Artikel
Sprache:eng
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Zusammenfassung:Four bis-lactam [ , +4]-stapled peptides with d- or l-α-methyl-thialysines were constructed on a model peptide sequence derived from p110α[E545K] and subjected to circular dichroism (CD) and proteolytic stability assessment, alongside the corresponding bis-lactam [ , +4]-stapled peptide with l-thialysine. The % α-helicity values of these four stapled peptides were found to be largely comparable to each other yet greater than that of the stapled peptide with l-thialysine. An l-α-methyl-thialysine-stapled peptide built on a model peptide sequence derived from ribonuclease A (RNase A) was also found to exhibit a greater % α-helicity than its l-thialysine-stapled counterpart. Moreover, a greater proteolytic stability was demonstrated for the l-α-methyl-thialysine-stapled p110α[E545K] and RNase A peptides than that of their respective l-thialysine-stapled counterparts.
ISSN:1420-3049
1420-3049
DOI:10.3390/molecules25194506