Peptide Inhibitors

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CAT#	Product Name	M.W	Molecular Formula	Inquiry
10-101-01	Tetracosactide Acetate	2933.5	C136H210N40O31S	Inquiry
10-101-07	Buserelin Acetate	1299.48	C62H90N16O15	Inquiry
10-101-14	Enfuvirtide	4492.01	C204H301N51O64	Inquiry
10-101-159	Dulaglutide	59669.8068	C2646H4044N704O836S18	Inquiry
10-101-182	Pexiganan acetate	2537.22596	C124H214N32O24	Inquiry
10-101-204	TFLLR-NH2(TFA)	761.83	C33H54F3N9O8	Inquiry
10-101-207	Gonadorelin diacetate	1302.39	C59H83N17O17	Inquiry
10-101-212	Thymosin β4 (1-4)	487.5	C20H33N5O9	Inquiry
10-101-218	Calcitonin	3414.87	C146H241N43O47S2	Inquiry
10-101-239	Annexin A1 (1-25) (dephosphorylated) (human)	3089.43	C141H210N32O44S	Inquiry
10-101-251	Ile-Pro-Pro	325.4	C16H27N3O4	Inquiry
10-101-256	FC131	729.8	C36H47N11O6	Inquiry
10-101-267	Arg-Gly-Asp	346.34	C12H22N6O6	Inquiry
10-101-269	C-Reactive Protein (CRP) (77-82)	560.61	C23H40N6O10	Inquiry
10-101-270	C-Reactive Protein (CRP) (174-185)	1276.51	C62H93N13O16	Inquiry
10-101-280	β-Casomorphin (1-7), bovine	789.92	C41H55N7O9	Inquiry
10-101-290	Fibrinopeptide B, human	1552.6	C66H93N19O25	Inquiry
10-101-291	Bradykinin 1-7	756.8	C35H52N10O9	Inquiry
10-101-292	Leptin Fragment 116-130 Amide mouse	1560.7	C64H109N19O24S	Inquiry
10-101-293	GLP-1(7-36) Acetate	3394.67	C149H226N40O45.xC2H4O2	Inquiry

Peptide inhibitors have the advantages of high affinity and specificity, low production cost, etc., and have attracted the attention of researchers.

Introduction of peptide inhibitors of PD-1/PD-L1 signaling pathway

Phage display technology is an efficient biological panning method that uses targets to screen high-affinity peptides and antibodies from libraries. Kotraiah et al. reported that four high-affinity phage clones were screened using recombinant human PD-1 protein, and the peptide sequence displayed on the surface of the phage was chemically synthesized to obtain PD-1 peptide. In vitro experiments proved that PD-1 peptide can bind to human PD-1 receptor and block PD-L1 binding; molecular simulation results showed that PD-1 peptide can bind to specific sites of PD-1 to exert biological activity. In vivo experiments proved that, PD-1 peptide had anti-melanoma metastasis ability similar to PD-1 mAb, increased the survival rate of lethal sepsis in mice, and can also be used as an immune adjuvant to improve the protective efficacy of preventive malaria vaccines. In addition, computer-aided peptide inhibitor design and peptide or peptidomimetic inhibitors designed based on PD1/PD-L1 functional fragments are also in progress.

Introduction to CCR5 and HIV gp120 peptide inhibitors

The role of CCR5 and gp120 has made it an attractive target for anti-HIV-1 drug research. Some polypeptides derived from the extracellular region of CCR5 and some antibodies can selectively interact with the surface glycoprotein of the virus and have the effect of inhibiting the fusion of the virus with cells. Yu Yong et al. designed a series of peptide analogues based on the crystal structure of a monoclonal antibody 17b that directly interacts with gp120, and selected a peptide P20 from them. By testing the ability of the polypeptide to inhibit virus entry, it was found that P20 has a significant ability to inhibit the entry of R5 HIV-1 into human peripheral blood mononuclear cells (PBMC), and had no significant effect on the entry of R4 HIV-1.

Introduction to L-JNK peptide inhibitor

L-JNK Peptide Inhibitor competitively blocks the interaction between JNK and c-Jun, thereby inhibiting the signaling events downstream of JNK, like c-Jun, ATF-2 and ELK1 phosphorylation. To convert JIP-1/IB-1 into cell permeable inhibitors of JNK (JNKI1) the minimal 20 amino acids inhibitory sequence of JIP-1/IB1 was covalently linked to the 10 amino acids recognized by TAT transporter. The L-JNKI1 is a potent inhibitor that is specific for JNK and can be used for in vitro applications.

It is worth noting that peptide inhibitors themselves also have disadvantages that need to be improved, such as instability in the body and poor membrane penetration ability. It has been reported in the literature that the combination of configuration transformation and nanotechnology can improve the efficacy of drugs. In addition, polypeptide structure modification, such as introduction of hydrophilic groups, side chain modification, cyclization, etc., can further improve its biological activity and druggability.

References

Kotraiah Vinayaka, Phares Timothy W, Browne Cecille D, et al. Novel Peptide-Based PD1 Immunomodulators Demonstrate Efficacy in Infectious Disease Vaccines and Therapeutics.[J]. Frontiers in Immunology, 2020, 11:264.
Yu Yong et al., Chinese Science Bulletin, 2004, 49(18): 1913-1914