Thrombin Receptor Activator Peptide 6 (TRAP-6) – CAS 141136-83-6

Thrombin Receptor Activator Peptide 6 (TRAP-6), also called Selective Protease-Activated Receptor 1 (PAR-1) Agonist, is an hexapeptide fragment of the thrombin receptor (residues 42-47).

TRAP-6 has been shown to selectively activate PAR1 and thus induce platelet aggregation (EC50 = 0.8 μM). Its usefulness has therefore been demonstrated in cardiovascular study models and in hematology.

Biologically, TRAP-6 is the N-terminal fragment of the thrombin receptor resulting from its cleavage by thrombin. This peptide therefore offers a cost-effective solution for the study of in-vitro cardiovascular models.

What is PAR-1 ?

Proteinase-activated receptor 1 (PAR1), also known as coagulation factor II (thrombin) receptor, is a G protein-coupled receptor and is involved in the regulation of thrombotic response. It is highly expressed in platelets and endothelial cells

Other Applications ?

Therefore, this peptide was used to activate platelets in vitro but it also demonstrated a protective action on astrocytes, which is associated with hypoglycemia.

Thus, some research has focused on the use of TRAP-6 peptide to study the pathways that regulate hypoglycemia. Others have also been interested in TRAP-6 because of its stimulating action on certain transcription regulators, notably the yes-associated protein (YAP).

Technical specification

TRAP-6 peptide buy Sequence : SFLLRN
TRAP-6 peptide synthesis MW : 748.87 g/mol (C34H56N10O9)
TRAP-6 peptide price Purity : > 95%
Peptide Library synthesis Counter-Ion : TFA Salts (see option TFA removal)
Peptide library synthesis TRAP-6 peptide Delivery format : Freeze dried in propylene 2mL microtubes
buy synthesized peptides Other Names : 141136-83-6, TRAP 6, Thrombin Receptor Activator Peptide 6, PAR1 agonist, Thrombin Receptor (1-6), Coagulation Factor II Receptor (1-6)
peptide solubility guidelines Peptide Solubility Guideline
buy peptide price Bulk peptide quantities available




Product catalog Size Price € HT Price $ USD
SB032-1MG 1 mg 77 96
SB032-5*1MG 5 mg 264 330



1- Gremmel T, Xhelili E, Steiner S, Koppensteiner R, Kopp CW, Panzer S. Atherosclerosis. (2014)
TRAP-6 peptide Response to Antiplatelet Therapy and Platelet Reactivity to Thrombin Receptor Activating peptide-6 in Cardiovascular Interventions: Differences Between Peripheral and Coronary Angioplasty


BACKGROUND : The long-term prognosis of patients with peripheral arterial disease (PAD) is significantly worse than the prognosis of coronary artery disease (CAD) patients. Detrimental platelet activation could contribute to the increased rate of adverse cardiovascular events in PAD. We therefore investigated whether response to antiplatelet therapy and thrombin inducible platelet activation differ between patients with best medical therapy undergoing angioplasty and stenting for symptomatic PAD (n = 166) or CAD (n = 104).

METHODS: Adenosine diphosphate (ADP), arachidonic acid (AA) and thrombin receptor activating peptide (TRAP)-6 inducible platelet reactivity was measured by multiple electrode aggregometry (MEA). Platelet surface expression of P-selectin and activated glycoprotein IIb/IIIa (GPIIb/IIIa) in response to ADP, AA, and TRAP-6, and the formation of monocyte-platelet aggregates (MPA) in response to ADP and TRAP-6 were assessed by flow cytometry.

RESULTS: Patients with PAD had significantly higher platelet reactivity in response to ADP and AA by MEA compared to CAD patients. Likewise, the expression of P-selectin and GPIIb/IIIa following stimulation with ADP and AA, and MPA formation in response to ADP were significantly higher in PAD patients than in CAD patients. In response to TRAP-6, patients with PAD showed a significantly increased platelet aggregation by MEA, higher expression of activated GPIIb/IIIa, and more pronounced formation of MPA than CAD patients.

CONCLUSION: Following angioplasty and stenting, PAD patients exhibit a significantly diminished response to dual antiplatelet therapy and an increased susceptibility to TRAP-6 inducible platelet activation compared to CAD patients

2- Gremmel T, Calatzis A, Steiner S, et al. Platelets. (2010)
TRAP-6 peptide Is TRAP-6 Suitable as a Positive Control for Platelet Reactivity When Assessing Response to Clopidogrel?



Adenosine 5′-diphosphate (ADP) inducible aggregation is used to assess platelet response to thienopyridines. Thrombin receptor-activating peptide-6 (TRAP-6) inducible aggregation may serve as a positive control because it acts via the thrombin receptor protease-activating receptor-1, which is not blocked by thienopyridines. We therefore investigated if TRAP-6 is suitable as a positive control when assessing residual platelet reactivity to ADP. Platelet response to clopidogrel was assessed in 200 patients on dual antiplatelet therapy using ADP inducible platelet aggregation by light transmission aggregometry (LTA), multiple electrode aggregometry (MEA), and the shear-dependent Impact-R. Test specificities were monitored by TRAP-6 inducible platelet aggregation. The aggregation-independent vasodilator-stimulated phosphoprotein (VASP) phosphorylation assay served for comparisons. ADP inducible aggregation was correlated to that by TRAP-6 (r = 0.33 to 0.72; p < 0.001 for all assays). A linear correlation was seen within MEA (r = 0.72). LTA TRAP-6 correlated weakly with the VASP assay (r = 0.19; p = 0.01), while there were no correlations of TRAP-6 responses by MEA or the Impact-R with the VASP assay (r = 0.03 and &#x2212;0.09; p > 0.05). In all three assays, differences between ADP and TRAP-6 inducible aggregation varied considerably. Within MEA, TRAP-6 inducible aggregation was almost always stronger than ADP inducible aggregation, while within LTA and the Impact-R, weak responses to ADP were associated with both, weak and strong responses to TRAP-6. In conclusion, the application of TRAP-6 as a positive control for platelet reactivity has major limitations and results need to be cautiously interpreted on an individual basis.

3- Ceruso MA, McComsey DF, Leo GC, et al. Bioorg Med Chem. (1999)
TRAP-6 peptide Thrombin Receptor-Activating Peptides (TRAPs): Investigation of Bioactive Conformations via Structure-Activity, Spectroscopic, and Computational Studies



The thrombin receptor (PAR-1) is an unusual transmembrane G-protein coupled receptor in that it is activated by serine protease cleavage of its extracellular N-terminus to expose an agonist peptide ligand, which is tethered to the receptor itself. Synthetic peptides containing the agonist motif, such as SFLLRN for human PAR-1, are capable of causing full receptor activation. We have probed the possible bioactive conformations of thrombin receptor-activating peptides (TRAPs) by systematic introduction of certain conformational perturbations, involving alpha-methyl, ester psi(COO), and reduced-amide psi(CH2N) scans, into the minimum-essential agonist sequence (SFLLR) to probe the importance of the backbone conformation and amide NH hydrogen bonding. We performed extensive conformational searches of representative pentapeptides to derive families of putative bioactive structures. In addition, we employed 1H NMR and circular dichroism (CD) to characterize the conformational disposition of certain pentapeptide analogues experimentally. Activation of platelet aggregation by our pentapeptide analogues afforded a structure-function correlation for PAR-1 agonist activity. This correlation was assisted by PAR-1 receptor binding data, which gauged the affinity of peptide ligands for the thrombin receptor independent of a functional cellular response derived from receptor activation (i.e. a pure molecular recognition event). Series of alanine-, proline-, and N-methyl-scan peptides were also evaluated for comparison. Along with the known structural features for PAR-1 agonist peptides, our work adds to the understanding of peptide topography relative to platelet functional activity and PAR-1 binding. The absolute requirement of a positively charged N-terminus for strong agonist activity was contradicted by the N-terminal hydroxyl peptide psi(HO)S-FLLR-NH2. The amide nitrogen between residues 1 and 2 was found to be a determinant of receptor recognition and the carbonyl groups along the backbone may be involved in hydrogen bonding with the receptor. Position 3 (P3) of TRAP-5 is known to tolerate a wide variety of side chains, but we also found that the amide nitrogen at this position can be substituted by an oxygen, as in SF-psi(COO)-LLR-NH2, without diminishing activity. However, this peptide bond is sensitive to conformational changes in that SFPLR-NH2 was active, whereas SF-NMeL-LR-NH2 was not. Additionally, we found that position 3 does not tolerate rigid spacers, such as 3-aminocyclohexane-1-carboxylic acid and 2-aminocycloalkane-1-carboxylic acid, as analogues 1A, 1B, 2A, 2B, 3, 4, 5A and 5B lack agonist activity. On the basis of our results, we suggest that an extended structure of the agonist peptide is principally responsible for receptor recognition (i.e. binding) and that hydrophobic contact may occur between the side chains of the second (Phe) and fourth (Leu) residues (i.e. P2-P4 interaction).