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MIF-1 (Pro-Leu-Gly-NH2) / Studies
Natural peptide · 3 amino acids · 284.4 Da

MIF-1 (Pro-Leu-Gly-NH2) studies and research data

PepBank has 89 MIF-1 studies with results. 87 of them gave MIF-1, with 317 results, grouped by what the studies measured. In each group, results from studies in people come first. Data as of 2026-10-30.

Searches 317 results and 144 papers. Newer studies from Europe PMC

Results in people
18
6% of 317 results
Results in animals
253
80% of 317 results
Results in lab cells
46
15% of 317 results
From computer models
0
0% of 317 results
The molecule

MIF-1 identity

Identifiers, parent molecule, targets and development stage, from curated data.

MIF-1 is Pro-Leu-Gly-NH2. It matches the amidated C-terminal three residues of oxytocin. It differs from macrophage migration inhibitory factor, longer melanostatin hormones, and modified MIF-1 analogs. The query requires neuropeptide context and excludes macrophage MIF naming.

Kind
Natural peptide · 3 residues
Identifiers
UniProtP01178 (opens in a new tab)PubChem CID92910 (opens in a new tab)UNII3KY24B4Q62 (opens in a new tab)CAS2002-44-0
Parent
Fragment of Oxytocin · residues 26-28PLG matches UniProt P01178 positions 26-28 and mature oxytocin positions 7-9. This structural relation alone does not establish a biosynthetic pathway.
Development
UnknownA formal clinical development phase was not established.

Targets

Molecular targets with action and evidence source
TargetActionEvidence
Dopamine D2 receptorPositive allosteric modulationPreclinical studies report increased dopamine agonist responses. PMID 10821635 reports PLG effects in rat striatal membranes. This does not establish clinical efficacy.Source (opens in a new tab)

Sequence and structure

Residues, differences from the parent, calculated properties and 3D structure. Source values and calculated values are shown separately.

Sequence

3 amino acids · 1 modification

H-
Residues 1 to 3:
PLG
  • HydrophobicA V I L M
  • SpecialC G P
  • Modified residue

Modifications

3
C-terminal amide
C-terminal carboxamide.

Alignment to Oxytocin

Calculated from the two sequences. Curated notes are shown as given.

3 of 3 aligned residues identical (100%) · 1 modified residue · Oxytocin 7–9

  • Top row: Oxytocin (parent)
  • Bottom row: MIF-1 (Pro-Leu-Gly-NH2)
PL
  • Same as parent
  • Substituted
  • Non-canonical or D-form
  • Added
  • Gap
  • Modified side chain or end
  • Parent context

Differences from the parent

  1. 1Parent 9 · analog 3Gly, modified · C-terminal amideC-terminal carboxamide.

Basis: PLG matches UniProt P01178 positions 26-28 and mature oxytocin positions 7-9. This structural relation alone does not establish a biosynthetic pathway.

Calculated from the two sequences with @pepdb/chem alignToParent (ungapped unless a gap scores higher). The record’s curated notes are shown as given.

Properties

From identity sources

Formula
C13H24N4O3
Molecular weight
284.35 g/mol
Monoisotopic mass
284.1848 Da

Calculated from the sequence

Average mass
284.36 Da
Sum of ExPASy residue masses + water + C-amide · ExPASy Compute pI/Mw; FindMod
Monoisotopic mass
284.1848 Da
Sum of ExPASy residue masses + water + C-amide · ExPASy FindMod
Isoelectric point (pI)
Not calculated
The net charge does not reach zero between pH 0 and 14 (the peptide has no acidic or no basic group in this model).
Net charge at pH 7.4
0.94
Henderson-Hasselbalch, EMBOSS pKa set · EMBOSS iep, Epk.dat
GRAVY (hydropathy)
0.600
Mean Kyte-Doolittle hydropathy · Kyte and Doolittle 1982
Positive: hydrophobic on average.
Extinction coefficient, 280 nm (Cys reduced)
0 M⁻¹ cm⁻¹
5500 x Trp + 1490 x Tyr · Pace et al. 1995 (ExPASy ProtParam)
No Trp or Tyr: absorbance at 280 nm cannot measure this peptide.
Instability index
6.67
Dipeptide instability weights (DIWV) · Guruprasad et al. 1990
40 or below: classed as stable (ExPASy).
Aliphatic index
130.0
Mole % A + 2.9 V + 3.9 (I + L) · Ikai 1980
Boman index
−1.95 kcal/mol
Mean solubility value (negated) · Boman 2003
2.48 or below: lower protein-binding potential (Boman).
Hydrophobic moment (μH)
Not calculated
The sequence is too short for this method.
  • Defined and validated for proteins; use with care for short peptides.
  • Assumes an ideal alpha helix. Many short peptides are not helical.

@pepdb/chem 0.2.0 · EMBOSS pKa set · ExPASy residue masses

Net charge by pH

Net charge at pH 7.4: 0.94

Point or use arrow keys

Net charge of MIF-1 (Pro-Leu-Gly-NH2) from pH 0 to 14 (EMBOSS pKa set). Net charge at pH 7.4: 0.94.−0.6−0.4−0.20+0.2+0.4+0.6+0.8+102468101214pHNet chargepH 7.4

Henderson-Hasselbalch, EMBOSS pKa set, C-amide. Calculated, not measured.

Show as table
pHNet charge
01.00
11.00
21.00
31.00
41.00
51.00
61.00
70.98
80.80
90.28
100.04
110.00
120.00
130.00
140.00

Composition

  • Hydrophobic33% (1)
  • Special67% (2)

3 residues. Each residue counts in one class; F and W count as aromatic.

A Ala0 · 0%
I Ile0 · 0%
L Leu1 · 33%
M Met0 · 0%
V Val0 · 0%
F Phe0 · 0%
W Trp0 · 0%
Y Tyr0 · 0%
H His0 · 0%
K Lys0 · 0%
R Arg0 · 0%
D Asp0 · 0%
E Glu0 · 0%
N Asn0 · 0%
Q Gln0 · 0%
S Ser0 · 0%
T Thr0 · 0%
C Cys0 · 0%
G Gly1 · 33%
P Pro1 · 33%

3D structure

PredictedAlphaFold DB · P01178

Loads the 3D viewer (3Dmol.js, about 150 KB) and the model file from AlphaFold DB (EMBL-EBI).

  • Very high (pLDDT > 90)
  • Confident (90 > pLDDT > 70)
  • Low (70 > pLDDT > 50)
  • Very low (pLDDT < 50)

Predicted model of the whole UniProt entry P01178, not an experimental structure of MIF-1 (Pro-Leu-Gly-NH2). MIF-1 (Pro-Leu-Gly-NH2) = residues 26–28.

AlphaFold DB, EMBL-EBI and Google DeepMind · CC BY 4.0

2D structure

Draws the structure in your browser with RDKit (about 2.3 MB, loaded once).

SMILES fromPubChem CID 92910(opens in a new tab)

CC(C)C[C@@H](C(=O)NCC(=O)N)NC(=O)[C@@H]1CCCN1
Results by area

What the studies measured

People first in each area, then animals, then lab cells. Counts are exact and come from studies that gave the peptide.

Trials and papers
Status and safety
Data