202411-07-2

Upstream product

• 202411-03-8 Boc-Ala-Arg(Tos)-Pro-Ala-Lys(Z)-OBzl 
• 15761-38-3 L-N-Boc-Ala 
• 114856-02-9 Boc-Ala-Lys(Z)-OBzl 
• 202411-01-6 Boc-Arg(Tos)-Pro-Ala-Lys(Z)-OBzl 
• 202410-99-9 Boc-Pro-Ala-Lys(Z)-OBzl 
• 68641-29-2 N^α-Boc-Pro-OBt 
• 13836-37-8 Boc-Arg(Tos)-OH 
• 15761-39-4 1-(tert-butoxycarbonyl)-L-proline 
• 105916-77-6 N^α-Boc-N^δ-tosyl-Arg-OBt 
• 66024-53-1 BOC-Ala-POBT 

Downstream Products

• 544477-25-0 cyclo-Ala-Arg(Tos)-Pro-Ala-Lys(Z) 

Relevant academic research and scientific papers

Synthesis and thrombolytic activity of fibrinogen fragment related cyclopeptides

In the modification of the fibrinogen fragment related sequences ARPAK, QRPAK GRPAK and KRPAK, the corresponding cyclo-ARPAK, cyclo-QRPAK, cyclo-GRPAK, and cyclo-KRPAK were prepared in the diluted solution. The bioassay in vivo indicated that the thrombolytic potencies of cyclo-ARPAK, cyclo-GRPAK, cyclo-QRPAK, and cyclo-KRPAK were significantly higher than that of ARPAK, QRPAK, GRPAK, and KRPAK. In water, the cyclopeptides were incubated with pepsin or trypsin at 37°C for 64 h. There was no degradation product observed, on the other hand, with the same condition, the peptides were completely hydrolyzed in 8 h. The relationships among the rigidity or the conformation and the thrombolytic activity in vivo and the stability to enzyme-induced hydrolysis in vitro of the cyclopeptides were discussed.

Studies on Hybrid Peptides of Fragments from Fibrinogen

In the present paper the hybrid peptides of P6A and RGD, namely ARPAKRGDS 17, ARPAKRGDV19, ARPAKRGDF 21, QRPAKRGDS 18, QRPAKRGDV 20 and QRPAKRGDF 22, were synthesized via the solution method, segment condensation and TFA/TFMS A-catalyzed deprotection (in