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GHRP-6

Growth Hormone Releasing Peptide-6, Growth hormone-releasing hexapeptide, His-D-Trp-Ala-Trp-D-Phe-Lys-NH2

A synthetic hexapeptide that stimulates growth hormone secretion by mimicking ghrelin and binding to GHS receptors in the pituitary gland.

Quick Stats
Studies 702
Trials 0
Formula C46H56N12O6
Overview Studies 702 Clinical Trials 0
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pubmed Oct 3, 2016

Use of Ultraviolet Photodissociation Coupled with Ion Mobility Mass Spectrometry To Determine Structure and Sequence from Drift Time Selected Peptides and Proteins.

Theisen. Alina A; Yan. Bin B; Brown. Jeffery M JM; Morris. Michael M; Bellina. Bruno B; Barran. Perd...

The paper describes a fancy laboratory method that uses a laser and ion‑mobility mass spectrometry to break apart and identify peptides, including GHRP‑6, but it does not provide any information about how GHRP‑6 works in the body or how to use it for health or performance.

pubmed Jul 18, 2017

A polypeptide-mediated synthesis of green fluorescent gold nanoclusters for Fe<sup>3+</sup> sensing and bioimaging.

Li. Hua H; Huang. Hong H; Feng. Jiu-Ju JJ; Luo. Xiliang X; Fang. Ke-Ming KM; Wang. Zhi-Gang ZG; Wang...

In this paper, growth hormone releasing peptide-6 (GHRP-6) is a bioactive polypeptide and acts as the reducing agent and capping ligand for synthesis of bright green fluorescent gold nanoclusters (GHRP-6-Au NCs) by a simple and environmental-friendly aqueous method, with the assistance of NaBr as the fluorescent sensitizer. The obtained GHRP-6-Au NCs had high fluorescent quantum yield (10.7%), and the fluorescence was strongly quenched by the existence of trace Fe<sup>3+</sup>. Thus, a new and highly sensitive sensor for the assay of Fe<sup>3+</sup> was constructed based on the analyte-induced fluorescent quenching mechanism. The sensor had a low detection limit of 1.4&#xb5;M (S/N=3) and a wide linear range of 2-1000&#xb5;M. Besides, GHRP-6-Au NCs exhibited low cytotoxicity and high biocompatibility for cell imaging.

pubmed Sep 28, 2014

Ghrelin inhibits BSCB disruption/hemorrhage by attenuating MMP-9 and SUR1/TrpM4 expression and activation after spinal cord injury.

Lee. Jee Y JY; Choi. Hae Y HY; Na. Won H WH; Ju. Bong G BG; Yune. Tae Y TY

Blood spinal cord barrier (BSCB) disruption after spinal cord injury (SCI) leads to secondary injury and results in apoptosis of neurons and glia, leading to permanent neurological deficits. Here, we examined the effect of ghrelin on BSCB breakdown and hemorrhage after SCI. After moderate weight-drop contusion injury at T9 spinal cord, ghrelin (80&#x3bc;g/kg) was administered via intraperitoneal injection immediately after SCI and then the same dose of ghrelin was treated every 6h for 1d. Our data showed that ghrelin treatment significantly inhibited the expression and activation of matrix metalloprotease-9 (MMP-9) at 1d after SCI. The increases of sulfonylurea receptor 1 (SUR1) and transient receptor potential melastatin 4 (TrpM4) expressions at 1h and 8h after SCI respectively were also alleviated by ghrelin treatment. In addition, both BSCB breakdown and hemorrhage at 1d after injury were significantly attenuated by ghrelin. In parallel, the infiltration of blood cells such as neutrophils and macrophages was inhibited by ghrelin treatment at 1d and 5d after SCI respectively. We also found that ghrelin receptor, growth hormone secretagogue receptor-1a (GHS-R1a), was expressed in the blood vessel of normal spinal tissue. Furthermore, the inhibitory effects of ghrelin on hemorrhage and BSCB disruption at 1d after SCI were blocked by GHS-R1a antagonist, [D-Lys-3]-GHRP-6 (3mg/kg). Thus, these results indicate that the neuroprotective effect by ghrelin after SCI is mediated in part by blocking BSCB disruption and hemorrhage through the down-regulation of SUR1/TrpM4 and MMP-9, which is dependent on GHS-R1a.

pubmed Jun 9, 2017

Azapeptide Synthesis Methods for Expanding Side-Chain Diversity for Biomedical Applications.

Chingle. Ramesh R; Proulx. Caroline C; Lubell. William D WD

Mimicry of bioactive conformations is critical for peptide-based medicinal chemistry because such peptidomimetics may augment stability, enhance affinity, and increase specificity. Azapeptides are peptidomimetics in which the &#x3b1;-carbon(s) of one or more amino acid residues are substituted by nitrogen. The resulting semicarbazide analogues have been shown to reinforce &#x3b2;-turn conformation through the combination of lone pair-lone pair repulsion of the adjacent hydrazine nitrogen and urea planarity. Substitution of a semicarbazide for an amino amide residue in a peptide may retain biological activity and add benefits such as improved metabolic stability. The applications of azapeptides include receptor ligands, enzyme inhibitors, prodrugs, probes, and imaging agents. Moreover, azapeptides have proven therapeutic utility. For example, the aza-glycinamide analogue of the luteinizing hormone-releasing hormone analogue Zoladex is a potent long-acting agonist currently used in the clinic for the treatment of prostate and breast cancer. However, the use of azapeptides was hampered by tedious solution-phase synthetic routes for selective hydrazine functionalization. A remarkable stride to overcome this bottleneck was made in 2009 through the introduction of the submonomer procedure for azapeptide synthesis, which enabled addition of diverse side chains onto a common semicarbazone intermediate, providing a means to construct azapeptide libraries by solution- and solid-phase chemistry. In brief, aza residues are introduced into the peptide chain using the submonomer strategy by semicarbazone incorporation, deprotonation, N-alkylation, and orthogonal deprotection. Amino acylation of the resulting semicarbazide and elongation gives the desired azapeptide. Since the initial report, a number of chemical transformations have taken advantage of the orthogonal chemistry of semicarbazone residues (e.g., Michael additions and N-arylations). In addition, libraries have been synthesized from libraries by diversification of aza-propargylglycine (e.g., A<sup>3</sup> coupling reactions, [1,3]-dipolar cycloadditions, and 5-exo-dig cyclizations) and aza-chloroalkylglycine residues. In addition, oxidation of aza-glycine residues has afforded azopeptides that react in pericyclic reactions (e.g., Diels-Alder and Alder-ene chemistry). The bulk of these transformations of aza-glycine residues have been developed by the Lubell laboratory, which has applied such chemistry in the synthesis of ligands with promising biological activity for treating diseases such as cancer and age-related macular degeneration. Azapeptide analogues of growth hormone-releasing peptide-6 (His-d-Trp-Ala-Trp-d-Phe-Lys-NH<sub>2</sub>, GHRP-6) have for example been pursued as ligands of the cluster of differentiation 36 receptor (CD36) and show promising activity for the development of treatments for angiogenesis-related diseases, such as age-related macular degeneration, as well as for atherosclerosis. Azapeptides have also been employed to make a series of conformationally constrained second mitochondria-derived activator of caspase (Smac) mimetics that exhibit promising apoptosis-inducing activity in cancer cells. The synthesis of cyclic azapeptide derivatives was used to make an aza scan to study the conformation-activity relationships of the anticancer agent cilengitide, cyclo(RGDf-N(Me)V), and its parent counterpart cyclo(RGDfV), which exhibit potency against human tumor metastasis and tumor-induced angiogenesis. Innovations in the synthesis and application of azapeptides will be presented in this Account, focusing on the creation and use of side-chain diversity in medicinal chemistry.

pubmed Mar 28, 2021

The CD36 Ligand-Promoted Autophagy Protects Retinal Pigment Epithelial Cells from Oxidative Stress.

Dorion. Marie-France MF; Mulumba. Mukandila M; Kasai. Shuya S; Itoh. Ken K; Lubell. William D WD; On...

This study looked at a CD36‑binding molecule (MPE‑001) that helps eye cells survive oxidative stress by boosting autophagy. It does not involve the peptide GHRP‑6, nor does it give any guidance that biohackers could apply to longevity, metabolism, or performance.