2016
DOI: 10.1039/c5cc09257d
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Foldameric probes for membrane interactions by induced β-sheet folding

Abstract: Design strategies were devised for    -peptide foldameric analogues of the antiangiogenic anginex with the goal of mimicking the diverse structural features from the unordered conformation to a folded  -sheet in response to membrane interactions. Structureactivity relationships were investigated in the light of different  -sheet folding levels.

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Cited by 4 publications
(3 citation statements)
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“…This result is important since, to the best of our knowledge, no examples of extended α,β 2,3 -foldamers are reported. Furthermore, there is a need of the development of bioactive proteolytically stable foldameric β-sheets that might be useful as modulators of protein-protein interactions (PPI) (Hegedüs et al, 2016). The design of this secondary structure is indeed not trivial, although β-sheet interfaces frequently occurred in PPI.…”
Section: Introductionmentioning
confidence: 99%
“…This result is important since, to the best of our knowledge, no examples of extended α,β 2,3 -foldamers are reported. Furthermore, there is a need of the development of bioactive proteolytically stable foldameric β-sheets that might be useful as modulators of protein-protein interactions (PPI) (Hegedüs et al, 2016). The design of this secondary structure is indeed not trivial, although β-sheet interfaces frequently occurred in PPI.…”
Section: Introductionmentioning
confidence: 99%
“…47 Systematic  3 -and ACHC-substitutions were done in the three-stranded Anginex structure, revealing that lipid-induced folding behavior as well as biologic activity can be retained with peripheral replacements (Figure 2a). 48,49 Another approach utilized amyloidogenic sequences to promote -sheet formation while using N-methyl amino acids to suppress H-bond formation, thus preventing aggregation. The structure was further stabilized by the formation of a macrocycle (Figure 2b).…”
Section: Design Of Secondary Structuresmentioning
confidence: 99%
“…Although neighborhood effects of the βand D-α-residues on the adjacent α-residues cannot be ruled out, our earlier observations demonstrated no major systematic influence preventing the chemical shift analysis. 48,49 The salt-dependent aggregation of the compounds was tested by measuring the The integrals were corrected for sample dilution and sensitivity loss caused by high salt concentration with the signal attenuation of a reference sample (2 mM glucose).…”
Section: Nmr Experimentsmentioning
confidence: 99%