Lot certificates published
Plain, secure packaging

Compound monograph

HNGF6A

HNGF6A is a synthetic humanin analog with F6A and S14G substitutions, described as non-IGFBP-3-binding in a comparative disposition study.

Published: 2026-09-16Literature/identifier verification: 2026-09-15
Also known asHNGF6AF6A/S14G-humanin

01

Identity & nomenclature

HNGF6A is a synthetic humanin analog with F6A and S14G substitutions, described as non-IGFBP-3-binding in a comparative disposition study.

HNGF6A is not an alias of humanin or HNG. F6A-humanin alone is a third molecule again — it retains Ser14. Some records collapse humanin and its derivatives under broad substance names, so the sequence must control assignment rather than the label.

Canonical name: [Ala6,Gly14]-humanin.

Declared aliases and development codes: HNGF6A, F6A/S14G-humanin.

02

Molecular properties

Molecular formulaC112H198N34O31S2
Molecular mass2581.1 Da
CAS Registry Number1093111-54-6
PubChem CID90489015
One-letter sequenceMAPRGASCLLLLTGEIDLPVKRRA
Terminal groupsFree N-terminus; Free C-terminal carboxyl

Twenty-four residues, free at both termini. Two substitutions relative to humanin: F6A and S14G. Chain length is unchanged, so '24-residue humanin analog' does not identify it.

03

Structural characteristics

A rodent study compared HNGF6A with HNG in wild-type animals and HNG in animals lacking IGFBP-3. Its non-IGFBP-3-binding designation defines the comparison; plasma humanin immunoreactivity does not establish intact-peptide identity. A separate study explicitly examined HNGF6A in isolated islets and cultured murine beta cells with scrambled-peptide controls and assessed K-ATP channel dependence. Those experimental systems do not establish a direct receptor assignment for this double-substituted peptide.

  • F6A
  • S14G

Terminal features: Free N-terminus, Free C-terminal carboxyl.

04

Molecular targets & mechanisms

05

Analytical considerations

Require fragments establishing BOTH Ala6 and Gly14; either alone leaves it indistinguishable from HNG or from F6A-humanin. Relative to HNG the F6A substitution removes C6H4, a calculated monoisotopic difference of 76.031 Da. Testing IGFBP-3 binding characterises function and cannot substitute for chemical identity — degradation, aggregation or assay failure would all produce an apparent absence of binding.

Disagreements and mix-ups

Points where sources disagree about this compound's identity, or where a name or form is easily confused with another, as noted in this record. The discrepancy register quotes the passage for each one.

What the studies reported

Each finding describes one cited study in its stated model. These observations are specific to that study and do not establish effects in other settings.

Cell and tissue studies

  • Isolated islets from normal mice

    Kuliawat et al. reported increased glucose-stimulated insulin secretion with HNGF6A in isolated islets from normal mice compared with scrambled peptide controls.

    Reference [2]
  • Isolated islets from diabetic mice

    Kuliawat et al. reported increased glucose-stimulated insulin secretion with HNGF6A in isolated islets from diabetic mice compared with scrambled peptide controls.

    Reference [2]

Animal studies

  • Male wild-type mouse pharmacokinetic model

    Chin et al. reported a longer plasma humanin-immunoreactivity half-life in male wild-type mice receiving HNGF6A than in wild-type mice receiving HNG, as measured by ELISA.

    Reference [1]
  • Three-month-old Sprague-Dawley rat hyperglycemic clamp model

    Kuliawat et al. observed a significantly higher glucose infusion rate and higher insulin levels during hyperglycemic clamps in three-month-old Sprague-Dawley rats receiving HNGF6A compared with saline controls.

    Reference [2]

06

Verified bibliography

Cited studies by type

The 2 papers this record cites, counted by the kind of work each reports. A count is the size of this record's selection, not of the research that exists, and says nothing about results, safety, effectiveness or approval.

A paper can report more than one kind of work. Each count opens those papers in the bibliography. Compare every record on the Evidence Map.

  1. Reference 1

    Pharmacokinetics and tissue distribution of humanin and its analogues in male rodents.

    Chin YP, Keni J, Wan J, Mehta H, Anene F, Jia Y, Lue YH, Swerdloff R, Cobb LJ, Wang C, Cohen P

    Endocrinology · 2013-07-08 · Journal Article

    current
  2. Reference 2

    Potent humanin analog increases glucose-stimulated insulin secretion through enhanced metabolism in the β cell.

    Kuliawat R, Klein L, Gong Z, Nicoletta-Gentile M, Nemkal A, Cui L, Bastie C, Su K, Huffman D, Surana M, Barzilai N, Fleischer N, Muzumdar R

    FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2013-08-30 · Journal Article

    current

Study models of these references

What kind of experiment each cited paper reports, taken from its abstract unless marked. Not a summary of results.

ReferenceStudy models
Chin YP et al. 2013Study models reported: animal (mouse, rat) · from the abstract
Kuliawat R et al. 2013Study models reported: in vitro; animal (rat) · from the abstract

Record history

Published 2026-09-16.

No changes to this record's content have been recorded since publication.

Each entry names the parts of this record that changed on that date. Changes to links between records and to catalogue links are not listed. This history covers the tracked record fields; study findings are not listed here.

Cite this record: Purely Peptides Research Library. HNGF6A. Published 2026-09-16. https://purelypeptides.org/research/compounds/hngf6a/

10

Methodology & citation verification

Reference identity is checked against official PubMed metadata. Local deterministic receipts bind each normalized title and canonical metadata record to its verification date. Scientific values remain absent when an authoritative source has not been verified.

Read the full methodology →