Abstract
b3-Homoarginine was synthesized to examine the effect of arginine side chains on b-peptides. CD spectra revealed the presence of a 314-helix in MeOH, which undergoes a transition to an unordered or less ordered conformation in aq. soln. The dispersion of the amide and side-chain NH protons was increased when moving from MeOH to a 3:1 MeOH/H2O mixt. b-Heptaarginine was obsd. to be capable of penetrating the cells and entering the nuclear compartments. [on SciFinder (R)]
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Mahajan, Y. R., Rueping, M., & Seebach, D. (2002). b-Homoarginine-containing b-peptides: structure and cell-penetrating ability. Peptides 2002, Proceedings of the European Peptide Symposium, 27th, Sorrento, Italy, Aug.31-Sept.6, 2002. Laboratorium fuer Organische Chemie der Eidgenoessischen Technischen Hochschule Zuerich,ETH-Hoenggerberg,Zurich,Switz.
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