Dihexa

For Laboratory Research Use Only — Not for Human or Veterinary Use.

Standard (< 1,000 vials)$250/kit

Volume (1,000+ vials)$190/kit

Quantity (kits)

= 10 vials

Minimum order: 100 vials total. Mix and match across all products.

I confirm this order is for laboratory research use only.For Laboratory Research Use Only — Not for Human or Veterinary Use. By checking this box you affirm this product will not be used for human or animal administration.

Specifications

CAS Number	1401708-83-5
Molecular Formula	C27H44N4O5
Molecular Weight	504.66 g/mol
Purity	≥98% (HPLC)
Form	Lyophilized Powder
Storage	-20°C, desiccated, protected from light
Reconstitution	Bacteriostatic water

Certificate of Analysis

Lot documentation

Every production lot is independently third-party tested. A batch-specific Certificate of Analysis — documenting HPLC purity, mass spectrometry identity confirmation, and net peptide content — is issued with every shipment. View a sample COA to see the format.

View Sample COA About our testing →

Research context

An N-acylated dipeptide derivative of the angiotensin IV scaffold, engineered for lipophilicity. It behaves as a small molecule rather than a peptide, including in how it dissolves.

Structure and molecular target

Dihexa, also designated PNB-0408, is N-hexanoyl-Tyr-Ile-(6)-aminohexanoic amide. Only two of its components are standard amino acids. A six-carbon acyl chain caps the N-terminus and a six-carbon aminohexanoic amide extends the C-terminus, so the molecule is a short peptide core flanked by two aliphatic chains rather than a peptide in the conventional sense.

The design derives from angiotensin IV, a hexapeptide fragment of the angiotensin cascade. The Tyr-Ile pair reproduces the portion of that scaffold associated with activity, and the two aliphatic extensions were added to raise lipophilicity and membrane permeability far above what the parent peptide achieves. At 505 daltons with substantial hydrocarbon content, it falls in the physicochemical range of a small organic molecule.

The reported target is the hepatocyte growth factor and c-Met receptor system. The literature describes the compound as interacting with hepatocyte growth factor and modulating dimerisation-dependent c-Met signalling, which is a mechanism of protein-protein interaction rather than of orthosteric receptor binding.

Findings in the published research literature

Cultured hippocampal neurons provide the most cited endpoint, with dendritic spine density and synapse formation quantified by imaging. Cell scattering assays in epithelial monolayers are the classical functional readout for hepatocyte growth factor signalling and appear in the mechanistic work, alongside c-Met phosphorylation by immunoblot.

Rodent behavioural work, principally spatial learning tasks, extends this into whole-animal models. The evidence base is concentrated: a large proportion of the primary literature originates from the group that developed the compound, and independent replication remains limited. That concentration is worth accounting for when designing an experiment around reported potency figures.

Analytical verification

This material is analysed as a small molecule, not as a peptide. Nuclear magnetic resonance is genuinely informative here in a way it is not for a long peptide chain, since every proton environment in a 505-dalton structure can be assigned, and the hexanoyl and aminohexanoyl chains give characteristic aliphatic signals that confirm both modifications directly.

Chromatographically it is far more retained than an ordinary peptide of similar mass. The two aliphatic chains require substantially higher organic content to elute, and a gradient designed for peptides may not reach it at all. Both amino acid residues carry stereocentres, so diastereomeric impurities from racemisation during synthesis are possible and are distinguished by chromatography rather than by mass.

Handling and storage

Solubility	Aqueous solubility is limited compared with unmodified peptides, a direct consequence of the two aliphatic chains. Concentrated stocks in the literature are commonly prepared in dimethyl sulfoxide or ethanol and then diluted into aqueous buffer.
Reconstitution	Add solvent slowly and allow time for the solid to dissolve fully rather than assuming rapid dissolution. Check for undissolved material before diluting, since a partly dissolved stock gives a concentration lower than calculated.
Storage	Lyophilised solid at -20C, desiccated and protected from light.
Stability	The amide bonds are stable and there is no oxidation-prone or disulfide-forming residue. Precipitation on dilution into aqueous buffer is the practical failure mode rather than chemical degradation.