Chemical and Biological Investigations of β‐Oligoarginines

  title={Chemical and Biological Investigations of $\beta$‐Oligoarginines},
  author={Dieter Seebach and Kenji Namoto and Yogesh R. Mahajan and Pascal Bindschaedler and Reiner Sustmann and Michael Kirsch and Neil S. Ryder and Markus Weiss and Markus Sauer and Christian Roth and Sabine Werner and Hans-Dietmar Beer and Christine Munding and Peter Walde and Matthias Richard Voser},
  journal={Chemistry \& Biodiversity},
In view of the important role arginine plays in living organisms as the free amino acid and, especially, as a residue in peptides and proteins, the homologous β‐homoarginines are central in our investigations of β‐peptides (Fig. 1). The preparation of β2‐homoarginine derivatives suitably protected for solution‐ or solid‐phase peptide syntheses is described with full experimental detail (9 and 12 in Scheme 1). The readily available Fmoc‐β3hArg(Boc)2‐OH is used for manual solid‐phase synthesis of… 

Enantiomeric and Diastereoisomeric (Mixed) L/ D‐Octaarginine Derivatives – A Simple Way of Modulating the Properties of Cell‐Penetrating Peptides

Seven of the 256 possible ‘mixed’ Flua‐L/D‐octaarginine amides, 4a–4g, were synthesized and shown to have half‐lives in heparine‐stabilized human plasma between 8 min and 5.5 h (Figs. 5 and 7).

On the Terminal Homologation of Physiologically Active Peptides as a Means of Increasing Stability in Human Serum – Neurotensin, Opiorphin, B27‐KK10 Epitope, NPY

The terminal homologation by CH2 insertion into the peptides mentioned in the title is described, and the structure of the peptide chain from the N‐ terminal to the C‐terminal stereogenic center is identical, andThe modified peptide is protected against cleavage by exopeptidases.

On the Mechanism of Eukaryotic Cell Penetration by α‐ and β‐Oligoarginines – Targeting Infected Erythro­cytes

Fluorescein‐labeled α‐ and β‐octaarginine amides were synthesized. The route, by which these oligoarginine (OA) derivatives enter cells (hepatocytes, fibroblasts, macrophages), was investigated by

β‐Peptidic Secondary Structures Fortified and Enforced by Zn2+ Complexation – On the Way to β‐Peptidic Zinc Fingers?

The correlation between β2-, β3-, and β2,3-amino acid-residue configuration and stability of helix and hairpin-turn secondary structures of peptides consisting of homologated proteinogenic amino

β‐peptoid “Foldamers”—Why the additional methylene unit?

  • C. Olsen
  • Biology, Chemistry
  • 2011
An overview of the data obtained for β‐peptoid‐containing peptide mimics as well as a discussion of the future challenges associated with this type of backbone modification are provided.

Searching for new cell-penetrating agents: hybrid cyclobutane-proline γ,γ-peptides.

The introduction of cyclobutane residues inside the sequence affords a good balance between charge and hydrophobicity, reducing the number of positive charges, which results in lower toxicity and similar cell-uptake properties when compared to previously described peptide agents.

Syntheses, Receptor Bindings, in vitro and in vivo Stabilities and Biodistributions of DOTA‐Neurotensin(8–13) Derivatives Containing β‐Amino Acid Residues – A Lesson about the Importance of Animal Experiments

The amount of specifically bound radioligand is rather low and is confirmed by PET‐imaging experiments with the tumor‐bearing mice and by comparison of the in vitro plasma stability with the ex vivo blood content of the two 68Ga complexes shows that they are rapidly cleaved in the animals.

ADME Investigations of Unnatural Peptides: Distribution of a 14C‐Labeled β 3‐Octaarginine in Rats

Data indicated that the distribution of the acetyl‐β‐octaarginine‐related radioactivity in the organs and tissues shifted over time, and β‐peptides bearing proteinogenic side chains are compared with peptides consisting entirely of D‐α‐amino acid residues.

Synthesis, Structure, and Biological Applications of α‐Fluorinated β‐Amino Acids and Derivatives

This review gives a broad overview of the state of play with respect to the synthesis, conformational properties, and biological activity of α‐fluorinated β‐amino acids and derivatives. General

Permeation through Phospholipid Bilayers, Skin‐Cell Penetration, Plasma Stability, and CD Spectra of α‐ and β‐Oligoproline Derivatives

Details are described of the previously mentioned observation that a hexa‐β3‐Pro derivative penetrates fibroblast cells, and the results of an extensive investigation of oligo‐L‐ and oligo-D‐α‐prolines are presented, as well as of oligospecific cell‐penetrating peptides (CPPs) across lipid bilayers.