148182-34-7

Usage

InChI:InChI=1/C44H59N5O8/c1-28(2)23-33(46-41(53)36(26-31-19-13-9-14-20-31)49-43(56)57-44(5,6)7)38(50)47-35(25-30-17-11-8-12-18-30)40(52)45-34(24-29(3)4)39(51)48-37(42(54)55)27-32-21-15-10-16-22-32/h8-22,28-29,33-37H,23-27H2,1-7H3,(H,45,52)(H,46,53)(H,47,50)(H,48,51)(H,49,56)(H,54,55)/t33-,34-,35-,36-,37-/m0/s1

Upstream product

• 1261486-37-6 Boc-Phe-Leu-Phe-Leu-Phe-O-t-Bu 
• 24424-99-5 di-tert-butyl dicarbonate 
• 16937-99-8 N-Boc-D-Leu 
• 13734-34-4 N-tert-butoxycarbonyl-L-phenylalanine 
• 146803-42-1 N-(fluorenylmethyloxycarbonyl)-L-leucinal 
• 146803-43-2 Fmoc-Phe-H 
• 63792-78-9 D-Leu-Phe-D-Leu-Phe-OMe 
• 63792-75-6 D-Leu-Phe-OMe 
• 2577-90-4 methyl (2S)-2-amino-3-phenylpropanoate 
• 7524-50-7 methyl (2S)-2-amino-3-phenylpropanoate hydrochloride 
• 128175-89-3 Boc-Phe-D-Leu-Phe-D-Leu-Phe-OMe 
• 128175-90-6 Boc-D-Leu-Phe-D-Leu-Phe-OMe 
• 37885-98-6 H-DLeu-Phe-OMe*HCl 
• 92463-61-1 Boc-D-Leu-Phe-OH 

Relevant academic research and scientific papers

d-Peptide analogues of Boc-Phe-Leu-Phe-Leu-Phe-COOH induce neovascularization via endothelial N-formyl peptide receptor 3

N-formyl peptide receptors (FPRs) are G protein-coupled receptors involved in the recruitment and activation of immune cells in response to pathogen-associated molecular patterns. Three FPRs have been identified in humans (FPR1–FPR3), characterized by different ligand properties, biological function and cellular distribution. Recent findings from our laboratory have shown that the peptide BOC-FLFLF (l-BOC2), related to the FPR antagonist BOC2, acts as an angiogenesis inhibitor by binding to various angiogenic growth factors, including vascular endothelial growth factor-A165 (VEGF). Here we show that the all-d-enantiomer of l-BOC2 (d-BOC2) is devoid of any VEGF antagonist activity. At variance, d-BOC2, as well as the d-FLFLF and succinimidyl (Succ)-d-FLFLF (d-Succ-F3) d-peptide variants, is endowed with a pro-angiogenic potential. In particular, the d-peptide d-Succ-F3 exerts a pro-angiogenic activity in a variety of in vitro assays on human umbilical vein endothelial cells (HUVECs) and in ex vivo and in vivo assays in chick and zebrafish embryos and adult mice. This activity is related to the capacity of d-Succ-F3 to bind FRP3 expressed by HUVECs. Indeed, the effects exerted by d-Succ-F3 on HUVECs are fully suppressed by the G protein-coupled receptor inhibitor pertussis toxin, the FPR2/FPR3 antagonist WRW4 and by an anti-FPR3 antibody. A similar inhibition was observed following WRW4-induced FPR3 desensitization in HUVECs. Finally, d-Succ-F3 prevented the binding of the anti-FPR3 antibody to the cell surface of HUVECs. In conclusion, our data demonstrate that the angiogenic activity of d-Succ-F3 is due to the engagement and activation of FPR3 expressed by endothelial cells, thus shedding a new light on the biological function of this chemoattractant receptor.

Fully enzymatic peptide synthesis using C-terminal tert-butyl ester interconversion

Chemoenzymatic peptide synthesis is potentially the most cost-efficient technology for the synthesis of short and medium-sized peptides with some important advantages. For instance, stoichiometric amounts of expensive coupling reagents are not required an

Conformational aspects of human formylpeptide receptor antagonists

The conformation of several Phe-D-Leu-Phe-D-Leu-Phe analogues was analyzed using infrared absorption and circular dichroism. Their effect on human neutrophils was verified by receptor binding and chemotaxis assays. The results demonstrate that the compounds examined prefer an ordered conformation (β-turn) in amphipatic environment, and that they are able to antagonize the neutrophil functions evoked by CHO-Met-Leu-Phe.