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- W2946397311 endingPage "1919" @default.
- W2946397311 startingPage "1919" @default.
- W2946397311 abstract "Cα to N substitution in aza-amino acids imposes local conformational constraints, changes in hydrogen bonding properties, and leads to adaptive chirality at the nitrogen atom. These properties can be exploited in mimicry and stabilization of peptide secondary structures and self-assembly. Here, the effect of a single aza-amino acid incorporation located in the upper β-strand at a hydrogen-bonded (HB) site of a β-hairpin model peptide (H-Arg-Tyr-Val-Glu-Val-d-Pro-Gly-Orn-Lys-Ile-Leu-Gln-NH2) is reported. Specifically, analogs in which valine3 was substituted for aza-valine3 or aza-glycine3 were synthesized, and their β-hairpin stabilities were examined using Nuclear Magnetic Resonance (NMR) spectroscopy. The azapeptide analogs were found to destabilize β-hairpin formation compared to the parent peptide. The aza-valine3 residue was more disruptive of β-hairpin geometry than its aza-glycine3 counterpart." @default.
- W2946397311 created "2019-05-29" @default.
- W2946397311 creator A5009661567 @default.
- W2946397311 creator A5039396963 @default.
- W2946397311 creator A5056827208 @default.
- W2946397311 creator A5083019962 @default.
- W2946397311 date "2019-05-18" @default.
- W2946397311 modified "2023-09-26" @default.
- W2946397311 title "Aza-Amino Acids Disrupt β-Sheet Secondary Structures" @default.
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- W2946397311 doi "https://doi.org/10.3390/molecules24101919" @default.
- W2946397311 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6572070" @default.
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