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For laboratory research use only. Not for human or veterinary use.
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Angiotensin IV-derived peptidomimetic
Also catalogued as PNB-0408, N-hexanoic-Tyr-Ile-(6)-aminohexanoic amide.
Dihexa is a peptidomimetic rather than a peptide, so it carries no residue count. Its core is the tyrosine–isoleucine pair from the N-terminus of angiotensin IV, capped at one end by a hexanoyl group and extended at the other by 6-aminohexanoic acid ending in a primary amide. Neither cap is an amino-acid residue, and the two together are what the name records.
Dihexa is a small synthetic molecule derived from angiotensin IV, the hexapeptide fragment of angiotensin II. Its structure keeps the tyrosyl-isoleucine unit at the angiotensin IV N-terminus and replaces the rest of the chain with two non-peptide extensions: a six-carbon acyl group on the tyrosine nitrogen, and a six-carbon aminohexanoyl amide on the isoleucine carboxyl.
The molecule was developed at Washington State University as part of a series of metabolically stabilised angiotensin IV analogues and carries the development code PNB-0408. It is prepared by chemical synthesis and has no natural source.
Dihexa is an investigational compound. It is not an approved drug in any jurisdiction.
Sun X, Deng Y, Fu X, et al. AngIV-Analog Dihexa Rescues Cognitive Impairment and Recovers Memory in the APP/PS1 Mouse via the PI3K/AKT Signaling Pathway. Brain Sciences 2021;11(11):1487.
Citation titles are reproduced verbatim from the journal record. A citation documents the molecule's published identity and history; it is not a claim about the material sold here.