Building beta-Peptide H10/12 Foldamer Helices with Six-Membered Cyclic Side-Chains: Fine-Tuning of Folding and Self-Assembly

Mandity, IM [Mándity, István (Gyógyszerkémia, g...), author] Department of Pharmaceutical Chemistry (USZ / FP); Fulop, L [Fülöp, Lívia (Neurodegeneratív ...), author] Department of Medical Chemistry (USZ / ÁOK); Vass, E [Vass, Elemér (szerves kémia, sp...), author] Laboratory for Chiroptical Structure Analysis (... (ELTE / ELU FoS / IC); Toth, GK [Tóth, Gábor (Peptidkémia), author] Department of Medical Chemistry (USZ / ÁOK); Martinek, TA ✉ [Martinek, Tamás (Gyógyszerkémia), author] Department of Pharmaceutical Chemistry (USZ / FP); Fulop, F [Fülöp, Ferenc (Kémia), author] Department of Pharmaceutical Chemistry (USZ / FP)

English Scientific Article (Journal Article)
Published: ORGANIC LETTERS 1523-7060 1523-7052 12 (23) pp. 5584-5587 2010
  • SJR Scopus - Biochemistry: D1
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    The ability of the beta-peptidic H10/12 helix to tolerate side-chains containing six-membered alicyclic rings was studied. cis-2-Aminocyclohex-3-ene carboxylic acid (cis-ACHEC) res dues afforded H10/12 helix formation with alternating backbone configuration. Conformational polymorphism was observed for the alternating cis-ACHC hexamer, where chemical exchange takes place between the major left-handed H10/12 helix and a minor folded conformation. The hydrophobically driven self-assembly was achieved for the cis-ACHC-containing helix which was observed as vesicles similar to 100 nm in diameter.
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    2020-08-08 22:23