Cell‐Penetrating Peptide Foldamers: Drug‐Delivery Tools

Oba, Makoto

doi:10.1002/cbic.201900204

Cited by 34 publications

(11 citation statements)

References 68 publications

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“…Altogether these results suggest that hybrid foldamer–peptide macrocycles extend the range of properties beyond what can be achieved with peptide macrocycles alone. Further investigation may concern the contribution of the foldamer segment to enhance the cell penetration of the peptide, 31 or to enhance the peptide's ability to bind to a protein target. Progress along these lines is being made and will be reported in due course.…”

Section: Discussionmentioning

confidence: 99%

Conformational interplay in hybrid peptide–helical aromatic foldamer macrocycles

et al. 2021

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Section: Discussionmentioning

confidence: 99%

Conformational interplay in hybrid peptide–helical aromatic foldamer macrocycles

et al. 2021

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“…In particular, the field of peptide‐based foldamers has gained considerable interest in medicinal chemistry to circumvent some of the issues of short peptides by increasing their conformational stability and their stability towards proteolysis [3,4] . This feature makes peptidomimetic foldamer chemistry an important resource for the design of cell penetrating peptides (CPP), [5–9] antimicrobial peptides (AMP) [10–12] and inhibitors of protein‐protein interactions (PPI) [13,14] …”

Section: Introductionmentioning

confidence: 99%

Introducing the Chiral Constrained α‐Trifluoromethylalanine in Aib Foldamers to Control, Quantify and Assign the Helical Screw‐Sense**

Bodero

Guitot

Lensen

et al. 2022

Chemistry A European J

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Oligomers of α-aminoisobutyric acid (Aib) are achiral peptides that adopt 3 10 helical structures with equal population of left-and right-handed conformers. The screwsense preference of the helical chain may be controlled by a single chiral residue located at one terminus. 1 H and 19 F NMR, X-ray crystallography and circular dichroism studies on new Aib oligomers show that the incorporation of a chiral quaternary α-trifluoromethylalanine at their N-terminus induces a reversal of the screw-sense preference of the 3 10 -helix compared to that of a non-fluorinated analogue having an lα-methyl valine residue. This work demonstrates that, among the many particular properties of introducing a trifluoromethyl group into foldamers, its stereo-electronic properties are of major interest to control the helical screw sense. Its use as an easy-to-handle 19 F NMR probe to reliably determine both the magnitude of the screw-sense preference and its sign assignment is also of remarkable interest.

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“…Since the reactions with B’ at lower catalyst loadings or lower temperatures retained conversion yields comparable to those of B , the introduction of side-chain hydrocarbon stapling is effective in enhancing the catalytic activity of peptides. These results provide useful information related to the recent progress of the E / Z -selective ring-closing metathesis of peptides [ 56 , 57 ], l -prolyl catalysts [ 58 , 59 , 60 ], and peptide foldamer [ 61 , 62 , 63 ]. Further studies including enantioselectivity improvement, an expansion of the reaction scope using catalyst B’ , as well as applications to cell-penetrating peptides [ 64 , 65 , 66 ] are ongoing in our laboratory.…”

Section: Resultsmentioning

confidence: 99%

Design and Synthesis of Helical N-Terminal l-Prolyl Oligopeptides Possessing Hydrocarbon Stapling

et al. 2020

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We designed and synthesized helical short oligopeptides with an l-proline on the N-terminus and hydrocarbon stapling on the side chain. Side-chain stapling is a frequently used method for the development of biologically active peptides. Side-chain stapling can stabilize the secondary structures of peptides, and, therefore, stapled peptides may be applicable to peptide-based organocatalysts. Olefin-tethered cis-4-hydroxy-l-proline 1 and l-serine 2 and 8, and (R)-α-allyl-proline 18 were used as cross-linking motifs and incorporated into helical peptide sequences. The Z- and E-selectivities were observed for the ring-closing metathesis reactions of peptides 3 and 11 (i,i+1 series), respectively, while no E/Z-selectivity was observed for that of 19 (i,i+3 series). The stapled peptide B’ catalyzed the Michael addition reaction of 1-methylindole to α,β-unsaturated aldehyde, which was seven times faster than that of unstapled peptide B. Furthermore, the high catalytic activity was retained even at lower catalyst loadings (5 mol %) and lower temperatures (0 °C). The circular dichroism spectra of stapled peptide B’ showed a right-handed helix with a higher intensity than that of unstapled peptide B. These results indicate that the introduction of side-chain stapling is beneficial for enhancing the catalytic activity of short oligopeptide catalysts.

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Cell‐Penetrating Peptide Foldamers: Drug‐Delivery Tools

Cited by 34 publications

References 68 publications

Conformational interplay in hybrid peptide–helical aromatic foldamer macrocycles

Conformational interplay in hybrid peptide–helical aromatic foldamer macrocycles

Introducing the Chiral Constrained α‐Trifluoromethylalanine in Aib Foldamers to Control, Quantify and Assign the Helical Screw‐Sense**

Design and Synthesis of Helical N-Terminal l-Prolyl Oligopeptides Possessing Hydrocarbon Stapling

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