107694-12-2

Upstream product

• 13139-15-6 N-tert-butoxycarbonyl-L-leucine 
• 69-96-5 Phenylserin 
• 3392-09-4 Boc-Leu-ONSu 
• 80182-99-6 β-hydroxyphenylalanine methyl ester hydrochloride 
• 896735-84-5 Boc-L-Leu-DL-Phe(β-OH)-OMe 

Downstream Products

• 107794-92-3 Boc-Leu-Δ^Z-Phe azlactone 
• 75186-23-1 N^α-t-Butoxycarbonyl-L-leucyl-α,β-dehydrophenylalanine azolactone 
• 896735-85-6 Boc-L-Leu-ΔPhe-(Aib)3-OMe 
• 663604-59-9 Boc-L-Leu-ΔPhe-Aib-NHPy 
• 117833-87-1 TFA*H-Leu-Δ^Z-Phe-OMe 
• 118141-37-0 Boc-Leu-Δ^Z-Phe-OMe 

Relevant academic research and scientific papers

Design of peptides with α,β-dehydro-residues: Synthesis, crystal structure and molecular conformation of a peptide N-tertiary-butyloxycarbonyl-L-Leu-ΔPhe-L-Ile-OCH3

In order to develop new design rules with dehydro-residues a peptide tertiary-butyloxycarbonyl-L-Leu-ΔPhe-L-Ile-OCH3 was synthesized. The synthesis was carried out in solution using azlactone procedure. The three-dimensional structure of the peptide was determined by X-ray diffraction method and refined to an R-factor of 0.065. The peptide adopts an unfolded S-shaped conformation with φ1 = -78.8(6)°, ψ1 = -28.5(7)°, ψ2 = 51.8(7)°, ψ 2 = 44.6(7)°, ψ3 = -93.7(7)°, ψ 3T = 21.5(7)°. This is the first example of a characteristic unfolded conformation of a peptide having ΔPhe at (i + 2) position with a single branched β-carbon residue. The side chain conformation of Ile with χ1,1 = 60.5(8)° χ1,2 = -66.7(7)° is not in a favourable form thus causing strong steric constraints. The crystal packing is stabilized by two intermolecular hydrogen bonds N1 - H1 ? O2′ = 2.936(6) A? and N3 - H3 ? O1′ = 3.096(6) A? and a number of van der Waals interactions involving side chains of Leu, ΔPhe and Ile as one block and the Boc groups from neighbouring peptide molecules as the second block.

C-terminal constrained phenylalanine as a pharmacophoric unit in peptide-based proteasome inhibitors

Here we report the synthesis and biological properties of peptide-based molecules bearing constrained analogues of phenylalanine at the C-terminal. Compounds were tested as proteasome subunits' inhibitors. Dehydro-peptides showed good inhibition, in particular against trypsin-like (T-L) proteasome activity while some C-terminal Tic-derivatives inhibit only caspase-like activity in enzymatic β1 subunits with a certain degree of efficacy. The best analogues of the series demonstrated good resistance to proteolysis and a capacity to permeate the cell membrane.

Chiroptical Transcription of Helical Information through Supramolecular Harmonization with Dynamic Helices

With biologically important "peptide bundling" as the motif, new chromophoric cyclic host 1 was designed, which consists of two zinc porphyrin units that are connected by dynamic peptide helices of nonameric aminoisobutyric acid (Aib) units. Upon inclusio

One-pot optical resolution of oligopeptide helices through artificial peptide bundling

The helical sense of the peptidic parts of a cyclodimeric zinc porphyrin host with helical oligopeptide units (1) determines whether a right- or left-handed oligopeptide guest (2) is selectively bound (see picture). In contrast, enantiomers of nonhelical

Design of peptides with α,β-dehydro-residues: Syntheses, crystal structures and molecular conformations of two δPhe-Trp containing peptides

The ΔPhe-Trp is a newly designed moiety that was found inducing a unique conformation in peptides. The peptides Boc-L-Val-ΔPhe-L-Trp-OCH3 (I) and Boc-L-Leu-ΔPhe-L-Trp-OCH3 (II) were synthesized by azlactone method in solution phase.

CONFORMATIONAL ANALYSIS OF AN ACTIVE CHEMOTACTIC PEPTIDE ANALOG CONTAINING Z-DEHYDROPHENYLALANINE AT POSITION 3

Formyl-Met-Leu-ΔZ-Phe-OMe, an analog of the chemotactic tripeptide Formyl-Met-Leu-Phe has been synthesized to evaluate the effect of substitution of α,β-dehydrophenylalanine on activity and conformation.The analog peptide shows high biological