How we drifted into peptide chemistry and where we have arrived at

  title={How we drifted into peptide chemistry and where we have arrived at},
  author={Dieter Seebach and Thierry Kimmerlin and Radovan {\vS}ebesta and Marino A. Campo and Albert K. Beck},
Beta-peptidic peptidomimetics.
This Account presents examples of beta-peptidic compounds binding, as agonists or antagonists (inhibitors), to (i) major histocompatibility complex (MHC) proteins (immune response), (ii) the lipid-transport protein SR-B1 (cholesterol uptake from the small intestine), (iii) the core of interleukin-8 ( inflammation), and (iv) the oncoprotein RDM2.
Semi-synthesis of cyclosporins.
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.
Preparation of the β3‐Homoselenocysteine Derivatives Fmoc‐β3hSec(PMB)‐OH and Boc‐β3hSec(PMB)‐OH for Solution and Solid‐Phase‐Peptide Synthesis and Selenoligation
The title compounds, 4 and 7, have been prepared from the corresponding α-amino acid derivative selenocystine (1) by the following sequence of steps: cleavage of the SeSe bond with NaBH4,
Synthesis and High-Resolution NMR Structure of a β3-Octapeptide with and without a Tether Introduced by Olefin Metathesis
Bridging between (i)- and (i+3)-positions in a β3-peptide with a tether of appropriate length is expected to prevent the corresponding 314-helix from unfolding (Fig. 1). The β3-peptide
Preparation of Protected β2‐ and β3‐Homocysteine, β2‐ and β3‐Homohistidine, and β2‐Homoserine for Solid‐Phase Syntheses
The Ser, Cys, and His side chains play decisive roles in the syntheses, structures, and functions of proteins and enzymes. For our structural and biomedical investigations of β-peptides consisting of
Spatial Screening for the Identification of the Bioactive Conformation of Integrin Ligands
The recently available crystal structure of the αVβ3-integrin head groups with the highly active cyclic peptide developed in the group confirmed the indirectly derived receptor bound conformation and now allows a structure-based design of new integrin ligands.
Investigation of the Interactions of β‐Peptides with DNA Duplexes by Circular Dichroism Spectroscopy
It is impossible, at this stage of the investigation, to make a safe proposal about the actual nature of the interaction of the structures(s) of the complexes, the formation of which is suggested by the CD spectra reported herein.


Synthesis and CD Spectra of β2-(3-Aza-peptides)
During the search for new secondary structures, the replacement of the Cβ CH2 groups of β-peptides by NR is envisaged, which leads to β2-(3-aza- peptides), which are of great interest, since they might form additional H-bonds via their sp3-nitrogens.
Modification of Cyclosporin A (CS): Generation of an enolate at the sarcosine residue and reactions with electrophiles
Strong bases (lithium diisopropylamide (LDA) or BuLi) convert cyclosporin A (CS) to hexalithio derivative containing a Li alkoxide, four Li azaenolate, and one Li enolate units. The Li6 compound is
Use of the Wolff Rearrangement of Diazo Ketones from Amino Acids as a synthetic method for the formation of oligonucleo‐peptides: A novel approach to chimeric biomolecules
With the analogous polymer-bound and protected oligonucleotide derivatives as amino nucleophiles, excellent yields were obtained with all chain lengths tested and the products were purified by reversed-phase HPLC and characterized by MALDI-TOF mass spectrometry.
Synthesis of3-Peptides and Mixeda/3-Peptides by Thioligation
The so-called native chemical ligation works well with β-peptides, producing larger β3- and α/β3-mixed peptides, including temperature and concentration dependence.
Further C‐Alkylations of Cyclotetrapeptides via Lithium and Phosphazenium (P4) Enolates: Discovery of a New Conformation
Four cyclotetrapeptides containing one (1, 2) or two (3, 4) chiral amino acids have been C-alkylated or C-hydroxyalkylated through Li+ or phosphazenium (P4 · H+) enolates. The reactions are
The Miraculous CD Spectra (and Secondary Structures?) ofβ-Peptides as They Grow Longer, Preliminary Communication
The recently improved conditions for solid-phase synthesis of β3-peptides by the Fmoc strategy were used to synthesize a β-tetracosapeptide (4, Scheme) composed of eight different β-amino acid
Preparation ofβ2-Homotryptophan Derivatives forβ-Peptide Synthesis
In view of the prominent role of the 1H-indol-3-yl side chain of tryptophan in peptides and proteins, it is important to have the appropriately protected homologs H-β2HTrpOH and H-β3HTrpOH (Fig.)
Solid Phase Synthesis of Peptide C-Terminal Thioesters by Fmoc/t-Bu Chemistry
A novel method for the solid phase synthesis of thioesters by the most prevalent Fmoc/t-Bu method, based on the use of a 3-carboxypropanesulfonamide safety-catch linker, which is fully stable to repetitive exposure to the basic conditions needed for FmOC cleavage.
C‐Alkylation of Sarcosine Residues in Cyclic Tetrapeptides via Lithium Enlates
The cyclic tetrapeptides cyclo(-Leu-Sar-Gly-), cyclo(-Val-Sar-Sar-Gly-), and cylco(-Meleu-Gly-D-Alasar-) have been synthesized from the component amino acids (BOP-Cl coupling), using the