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HEMORPHIN-7

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Reduces Blood Pressure

Hemorphin-7 is a hemorphin peptide, an endogenous opioid peptide derived from

the chain of hemoglobin. Hemorphin peptides exhibit antinociceptive and

antihypertensive activities, activating opioid receptors and inhibiting angiotensinconverting enzyme (ACE).

It binds to the Amgiotensin receptor triggering multiple effects including cellular

prolifearation, preferentially interacts with delta and kappa receptors. It protentiates

the activity of bradykirin causing a decrease in blood pressure.

Benefits:

Increase the blood plasma

levels of immunoreactive

hemorphin-7

• Anti-inflammatory response

in acute and chronic injuries

• Reduces Blood Pressure

• Supports oxygen transport

from lung to various

peripheral tissues

• Reduce stiffness and aids in

flexibilty

Hemorphin-7 (HE7)

Purity: > 95%

Molecular Formula: C49H64N12O11 Molecular Weight: 997.110

Sequence (three-letter code): {TYR}{PRO}{TRP}{THR}{GLN}{ARG}{PHE}

Hemorphins are opioid peptides derived by proteolysis from hemoglobin. Their sequences are

identical in several mammalian species including horses and camels. LVV-hemorphin 7

(LVVYPWTQRF) binds strongly to the Angiotensin IV (AT4) receptors in the brain. The AT4

receptors is an integral membrane aminopeptidase also as IRAP (insulin-regulated membrane

aminopeptidase). LVV-hemorphin 7 and AT4 are not substrates but rather inhibitors of the AT4

(IRAP) receptor. Both promote learning and memory and reverse amnesia in animal models.

Elevated serum levels of LVV Hemorphin 7 have also been documented in animals associated with

an increased expression of Cathespins B and D.

ADMINISTRATION AND DOSAGE

Use 1 vial mixed with 2.5ml sterile water, sub-contaneus (under the skin). For best results use 1x

5mg vial every 5 days for 6 treatments.

INGREDIENTS

6x5mg HEMORPHIN-7 (99%).

STORAGE

Keep Refrigerated when possible and out of direct sunlight.

Clinical Research

In the current study, a series of alanine-substituted and N- or C-terminally modified analogs of LVVhemorphin-7 were evaluated for their abilities to compete for 125I-Ang IV binding in horse adrenal

and cerebellar membranes.

Selected analogs were also analyzed for binding to recombinant human IRAP and inhibition of

IRAP aminopeptidase activity. C-Terminal deletions of LVV-hemorphin-7 resulted in modest

changes in affinity for IRAP, whereas deletion of the first three N-terminal residues abolished

binding. Monosubstitutions of Tyr4 and Trp6 with alanine resulted in a 10-fold reduction in affinity.

Competition binding studies using recombinant horse IRAP demonstrated the same rank order of

affinity as obtained for the ovine tissues. All LVV-hemorphin-7 analogs tested, except for Leu-ValVal-Tyr, inhibit the cleavage of the synthetic substrate, leucine -naphthylamide, by IRAP,with Ki

values between 56 and 620 nM. We find that the Val3 residue is crucial for LVV-hemorphin-7

binding to IRAP, whereas the C-terminal domain seems to play a minor role. The current study

highlights the minimal residues necessary for binding and inhibition of IRAP and provides a basis to

design peptidomimetic analogs for experimental and potentially clinical use.
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HEMORPHIN-7