@inproceedings{980c31b421184a82a686ff31dbb736a1,
title = "β-Homoarginine-Containing β-Peptides: structure and cell-penetrating ability",
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)]",
keywords = "ABILITY, AMIDE, CELL, CELLS, CHAIN, CHAINS, CONFORMATION, Cd Spectra, Chemical, PROTEIN, SPECTRA, Structure, homoarginine beta peptide prepn heptaarginine cell",
author = "Mahajan, {Yogesh R} and Magnus Rueping and Dieter Seebach",
year = "2002",
language = "English (US)",
series = "Peptides 2002, Proceedings of the European Peptide Symposium, 27th, Sorrento, Italy, Aug.31-Sept.6, 2002",
booktitle = "β-Homoarginine-Containing β-Peptides: structure and cell-penetrating ability",
}