Dihexa
Also known as N-hexanoic-Tyr-Ile-(6) aminohexanoic amide, PNB-0408
Dihexa is an angiotensin IV–derived peptidomimetic studied in synaptogenesis research. A research-use profile: its angiotensin lineage, its unusual small structure, and handling.
Dihexa sits at the boundary between peptide and small molecule, and that is the most important thing to understand about it. It descends from angiotensin IV — a hexapeptide fragment of the angiotensin system that, separate from blood-pressure biology, has been studied in the context of the hepatocyte growth factor / c-Met system and synapse formation.
But Dihexa is not angiotensin IV. Chemists stripped that six-residue parent down to a minimal Tyr-Ile core and flanked it with fatty-acid-like caps — a hexanoyl group at one end and a 6-aminohexanoic amide at the other. Those aliphatic chains make the molecule far more lipophilic than a typical short peptide, which is precisely why it is described as a peptidomimetic rather than a straightforward peptide.
Because its structure is dominated by non-standard building blocks rather than a clean run of coded residues, this page does not present a residue sequence. It sticks to lineage, structure class, and the research settings the compound appears in.
Dihexa is a small peptidomimetic derived from angiotensin IV (the Val-Tyr-Ile-His-Pro-Phe hexapeptide). It reduces that parent to a two-residue Tyr-Ile core flanked by a hexanoyl group and a 6-aminohexanoic amide — the fatty-chain caps are what push it toward greater lipophilicity than a native peptide.
The angiotensin IV lineage
Angiotensin IV is the fragment that gives Dihexa its research context. Independent of the renin-angiotensin system's cardiovascular role, angiotensin IV has been examined in neuroscience for its interaction with the HGF/c-Met axis, a signaling pathway associated with synapse formation. Dihexa was engineered as a metabolically hardened, more lipophilic derivative of that fragment for study in the same synaptogenesis-focused research.
The design goal was a molecule that keeps the pharmacophore of interest from angiotensin IV while behaving very differently from a fragile hexapeptide — hence the fatty-chain caps and the collapse to a two-residue core.
Why it isn't a conventional peptide
A conventional research peptide is a chain of standard amino acids you can spell out three letters at a time. Dihexa instead couples a Tyr-Ile dipeptide to a hexanoyl cap and a 6-aminohexanoic-acid amide. The 6-aminohexanoic component is not one of the twenty coded amino acids, and the hexanoyl group is a fatty acyl chain — so the molecule reads more like a peptidomimetic than a peptide.
This structure is why Dihexa's certificate of analysis and mass will not resemble those of the short natural-sequence peptides it is often listed beside. Verify identity against its own reported structure and batch, not by analogy to a residue count.
Research contexts
In the literature Dihexa appears in synaptogenesis and neural-plasticity research and in work on the HGF/c-Met signaling system. These are the experimental areas it is associated with; the page describes where it has been studied, not any effect promised to a person.
These are research areas the compound is associated with in the literature — not medical claims or intended uses.
Handling & storage
Supplied lyophilized. Its lipophilic character means reconstitution practices can differ from those of standard hydrophilic peptides; in research settings it is prepared per the working protocol and kept cold and sealed. Handle per accepted laboratory practice.
Verify a certificate by lot →Common questions
It is a peptidomimetic derived from angiotensin IV, a hexapeptide fragment of the angiotensin system studied — apart from blood-pressure biology — in the context of the HGF/c-Met pathway and synapse formation.
Not in the usual sense. It reduces angiotensin IV to a Tyr-Ile core flanked by a hexanoyl cap and a 6-aminohexanoic amide, so it behaves more like a small peptidomimetic than a standard-residue peptide.
The fatty-acyl caps (a hexanoyl group and a 6-aminohexanoic amide) give it a markedly more lipophilic character than a typical short hydrophilic peptide — a defining feature of its design.
This monograph is a research-use reference. It describes composition and the contexts in which the compound has been studied — it is not medical advice, a description of effects, or a recommendation for use. Sold strictly for laboratory and research use; not for human or animal consumption.