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Compound monograph

HNG ([Gly14]-Humanin)

HNG is a synthetic single-substitution analog of humanin carrying glycine in place of serine at position 14.

Published: 2026-09-16Literature/identifier verification: 2026-09-15
Also known asHNGS14G-humaninS14G-HNHumanin-G

01

Identity & nomenclature

HNG is a synthetic single-substitution analog of humanin carrying glycine in place of serine at position 14.

HNG, S14G-HN and [Gly14]-humanin name the same substitution. 'Humanin-G' denotes substitution at position 14, not a glycine extension. HNGF6A additionally replaces Phe6 with alanine. These synthetic analogs require sequence-specific attribution; mitochondrial family membership does not establish endogenous expression.

Canonical name: [Gly14]-humanin.

Declared aliases and development codes: HNG, S14G-humanin, S14G-HN, Humanin-G.

02

Molecular properties

Molecular formulaC118H202N34O31S2
Molecular mass2657.2 Da
CAS Registry Number330936-70-4
PubChem CID16135997
One-letter sequenceMAPRGFSCLLLLTGEIDLPVKRRA
Terminal groupsFree N-terminus; Free C-terminal carboxyl

Twenty-four residues, free at both termini. Identical to humanin except at position 14, where serine is replaced by glycine.

03

Structural characteristics

Cell-binding experiments tested biotin-labeled humanin and HNG separately; receptor-subunit knockdown reduced HNG binding, and reconstituted-protein assays examined both peptides. In a separate biophysical study, HNG and SHLP2 associated with misfolded IAPP seeds. Fluorescence and co-sedimentation supported seed binding, while EPR and circular dichroism did not support binding to IAPP monomers. Rodent disposition experiments compared HNG with HNGF6A and included an IGFBP-3-deficient group; plasma measurements used a humanin ELISA, so immunoreactivity is distinct from intact-peptide identification.

  • S14G

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

04

Molecular targets & mechanisms

05

Analytical considerations

Verify glycine at position 14 with fragments spanning it. Relative to humanin the substitution removes CH2O, a calculated monoisotopic difference of 30.011 Da — small, and a fragment that omits position 14 cannot distinguish the two molecules at all. A humanin immunoassay or a shared biological response cannot establish which analog was supplied.

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

  • Cell-free IAPP thioflavin T fluorescence assay

    Okada et al. observed inhibition of IAPP misfolding by HNG at substoichiometric concentrations in a cell-free thioflavin T fluorescence assay.

    Reference [3]
  • Cell-free IAPP binding and seeding assays

    Okada et al. reported that HNG blocked IAPP amyloid seeding and bound misfolded, seeding-capable IAPP species in fluorescence and co-sedimentation assays.

    Reference [3]
  • Cell-free IAPP electron paramagnetic resonance and circular dichroism assays

    Okada et al. did not detect direct binding of HNG to IAPP monomers under the tested conditions in cell-free electron paramagnetic resonance and circular dichroism assays.

    Reference [3]

Animal studies

  • Adult male Sprague Dawley rat tissue-distribution model

    Chin et al. reported that after HNG exposure in adult male Sprague Dawley rats, humanin immunoreactivity was highest in plasma, was present in liver and was undetectable in brain or heart by ELISA.

    Reference [2]
  • Male wild-type mouse plasma-hormone model

    Chin et al. observed decreases over time in plasma IGF-1 and IGFBP-3 levels after HNG exposure in male wild-type mice.

    Reference [2]

06

Verified bibliography

Cited studies by type

The 3 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

    Humanin inhibits neuronal cell death by interacting with a cytokine receptor complex or complexes involving CNTF receptor alpha/WSX-1/gp130.

    Hashimoto Y, Kurita M, Aiso S, Nishimoto I, Matsuoka M

    Molecular biology of the cell · 2009-04-22 · Journal Article

    current
  2. Reference 2

    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
  3. Reference 3

    The Mitochondrial-Derived Peptides, HumaninS14G and Small Humanin-like Peptide 2, Exhibit Chaperone-like Activity.

    Okada AK, Teranishi K, Lobo F, Isas JM, Xiao J, Yen K, Cohen P, Langen R

    Scientific reports · 2017-08-10 · 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
Hashimoto Y et al. 2009Study models reported: in vitro · from the abstract
Chin YP et al. 2013Study models reported: animal (mouse, rat) · from the abstract
Okada AK et al. 2017Study models reported: in vitro · from the abstract

Compare

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. HNG ([Gly14]-Humanin). Published 2026-09-16. https://purelypeptides.org/research/compounds/hng/

10

Methodology & citation verification

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