329191-64-2

Upstream product

• 13500-53-3 N-benzyloxycarbonyl-(2S,4R)-4-hydroxyproline benzyl ester 
• 13504-86-4 (2S,4S)-1-benzyloxycarbonyl-4-hydroxyproline 
• 618-27-9 hydroxy L-proline 
• 13504-85-3 (2S,4R)-1-(benzyloxycarbonyl)-4-hydroxypyrrolidine-2-carboxylic acid 
• 501-53-1 benzyl chloroformate 
• 51-35-4 4R-4-hydroxyproline 
• 100-39-0 benzyl bromide 
• 329191-63-1 (2S,4S)-N^α-Cbz-4-bromoproline benzyl ester 

Downstream Products

• 329191-68-6 (2S,4R)-N^α-Cbz-4-N,N'-di-Boc-guanidinoproline benzyl ester 
• 329191-66-4 (2S,4R)-N^α-Cbz-4-aminoproline benzyl ester 

Relevant academic research and scientific papers

Structural development of cell-penetrating peptides containing cationic proline derivatives

We designed and synthesized a series of cell-penetrating peptides containing cationic proline derivatives (ProGu) that exhibited responsive changes in their secondary structures to the cellular environment. Effects of the peptide length and steric arrangement of the side chain in cationic proline derivatives [Pro4SGu and Pro4RGu] on their secondary structures and cell membrane permeability were investigated. Moreover, peptides 3 and 8 exhibited efficient intracellular delivery of plasmid DNA.

Design and synthesis of fluorinated peptides for analysis of fluorous effects on the interconversion of polyproline helices

The unique interaction between fluorine atoms has been exploited to alter protein structures and to develop synthetic and analytical applications. To expand such fluorous interaction for novel applications, polyproline peptides represent an excellent molecular nanoscaffold for controlling the presentation of perfluoroalkyl groups on their unique secondary structure. We develop approaches to synthesis fluorinated peptides to systematically investigate how the number, location and types of the fluorous groups on polyproline affect the conformation by monitoring the transition between the two major polyproline structures PPI and PPII. This work provides valuable information on how fluorous interaction affects the peptide structure and also benefits the design of functional fluorous molecules.

Novel μ opioid antagonists derived from the μ opioid agonists endomorphin and [Dmt1]DALDA (H-Dmt-D-Arg-Phe-Lys-NH2)

Hybrid analogues of the μ opioid agonists endomorphin and [Dmt1]DALDA (H-Dmt-D-Arg-Phe-Lys-NH2, Dmt?=?2′,6′-dimethyltyrosine) containing cis-4-amino-Pro, trans-4-amino-Pro, cis-4-aminoethyl-Pro or cis-4-guanidinylethyl-Pro in the 2 p