Peptide Schedule
Beta-Endorphin31 residuesYGGFMTSEKSQTPLVTLFKNAIIKNAYKKGEEach bubble = one amino acid. Size = residue mass. Color = chemical class.Beta-Endorphin Dosage Calculator
Beta-endorphin is the principal endogenous opioid peptide of the human body, first isolated and characterized by Choh Hao Li and David Chung in 1976 from camel pituitary extracts.
100mcg · EOD
Summary: Add 2mL BAC water to your 1mg vial. Draw to 20.0 units on a U-100 syringe for a 100mcg dose. This vial will last 10 doses.
Cycle Planner
Beta-Endorphin Pharmacokinetics
Pharmacokinetics — Active Dose Over Time
t½ = ~20-35 minutes (plasma); variable CNS half-lifeDisclaimer: This curve is a simplified first-order exponential decay model. Actual pharmacokinetics vary based on injection site, individual metabolism, body composition, and other factors. Half-life values are approximate and based on available preclinical and clinical literature. Many research peptides lack formal human pharmacokinetic studies. This is for educational purposes only — not medical advice.
Beta-Endorphin Dosing Protocol
| Level | Dose / Injection | Frequency |
|---|---|---|
| Beginner | 100mcg | EOD |
| Moderate | 250mcg | EOD |
| Aggressive | 500mcg | Daily |
Note: Beta-endorphin is a 31-amino-acid endogenous opioid neuropeptide (sequence: Tyr-Gly-Gly-Phe-Met-Thr-Ser-Glu-Lys-Ser-Gln-Thr-Pro-Leu-Val-Thr-Leu-Phe-Lys-Asn-Ala-Ile-Ile-Lys-Asn-Ala-Tyr-Lys-Lys-Gly-Glu) cleaved from the C-terminal fragment of pro-opiomelanocortin (POMC). It is the most potent endogenous analgesic produced by the human body, with approximately 18-33 times the analgesic potency of morphine on a molar basis. Beta-endorphin binds preferentially to mu-opioid receptors but also interacts with delta-opioid receptors. It is synthesized primarily in the anterior pituitary gland and arcuate nucleus of the hypothalamus and released into both the bloodstream and cerebrospinal fluid during stress, pain, and vigorous exercise. Exogenous administration remains strictly investigational. This entry is for research and educational reference only.
About Beta-Endorphin
Beta-endorphin is the principal endogenous opioid peptide of the human body, first isolated and characterized by Choh Hao Li and David Chung in 1976 from camel pituitary extracts. It comprises the 31-amino-acid C-terminal fragment (residues 237-267) of the 267-amino-acid precursor protein pro-opiomelanocortin (POMC), which also gives rise to ACTH, alpha-MSH, and other bioactive peptides through tissue-specific proteolytic processing. In the anterior pituitary, POMC cleavage by prohormone convertase 1 (PC1) yields ACTH and beta-lipotropin, with further cleavage of beta-lipotropin producing beta-endorphin. In the arcuate nucleus of the hypothalamus, additional processing by PC2 generates alpha-MSH and beta-endorphin that project widely throughout the central nervous system. Beta-endorphin binds mu-opioid receptors with nanomolar affinity (Ki approximately 1-3 nM) and delta-opioid receptors with somewhat lower affinity. It is considered the body's most powerful endogenous pain-relieving molecule, playing a central role in stress-induced analgesia, reward circuitry modulation, and neuroendocrine regulation. Plasma beta-endorphin levels rise dramatically during acute physical stress, intense exercise (the so-called "runner's high"), labor and delivery, and acute trauma. Cerebrospinal fluid levels correlate with analgesic states and mood regulation. Beyond pain modulation, beta-endorphin influences immune function by modulating natural killer cell activity and lymphocyte proliferation, regulates appetite through hypothalamic feeding circuits, and participates in the reward and reinforcement pathways that overlap with those activated by exogenous opioids. Dysregulation of the beta-endorphin system has been implicated in conditions including chronic pain syndromes, major depression, addiction, obesity, and fibromyalgia. As an exogenous therapeutic agent, beta-endorphin remains in the preclinical and research-only phase. Its rapid enzymatic degradation by aminopeptidases and enkephalinases in plasma limits peripheral bioavailability, and the blood-brain barrier restricts CNS access from systemic administration. Research interest focuses on understanding its physiological roles, developing stabilized analogs, and exploring potential applications in pain management and mood disorders.