pe
pep-10530 v1 CC-BY-SA-4.0

Brain-protective peptide found in injured rat brain (BINP)

A small peptide discovered in damaged brain tissue that helps nerve cells survive and shields them from toxic injury in lab studies; experimental, not yet an approved drug.

statuscomputed targetNPBWR1 length13 aa refs4
snapshot in_vitro 0% confidence
Class
Experimental neuropeptide
Status
No approved therapeutic status identified
Best-supported effect
Neuronal survival promotion in neonatal rat primary cell cultures (in vitro)
Main caveat
Evidence is limited to cell culture assays; no in vivo animal or human data are present in this card's source file
status 2 / 5
prediction metrics boltz-2 2.2.1
ipTM0.954
pTM0.926
avg pLDDT86.6
ranking score0.883
STRUCTURE · PEP-10530 × NPBWR1
ranking0.883
target interface 4.5Å peptide drag rotate · ctrl+scroll zoom · right-click pan
boltz-2 2.2.1 · mmCIF ↓ download
sequence13 aa
151013
EALELARGAIFQA
overview readme

Snapshot

Class: Experimental neuropeptide
Evidence tier: In vitro / assay evidence
Status: No approved therapeutic status identified
Best-supported effect: Neuronal survival promotion in neonatal rat primary cell cultures (in vitro)
Main caveat: Evidence is limited to cell culture assays; no in vivo animal or human data are present


What this is

BINP (Brain Injury Derived Neurotrophic Peptide) is a synthetic 13-amino-acid peptide originally isolated from traumatized rat brain tissue. In primary cell culture experiments, it promoted the survival of septal cholinergic neurons and mesencephalic dopaminergic neurons derived from neonatal rats, and protected cultured neurons from glutamate-induced injury. No in vivo animal studies or human data are present.


Evidence map

Evidence layerGradeWhat it supports
HumanNone identifiedNo human evidence present
AnimalNone identifiedNo in vivo animal evidence present
In vitroWeakNeuronal survival promotion and glutamate-injury rescue in neonatal rat primary cell cultures (one published study)
ComputationalNone identifiedNo computational or structural prediction data present
MechanismPlausibleNeurotrophic activity proposed based on cell culture observations; molecular target not specified in source

Claim check

ClaimVerdictEvidence layerConfidence
Promotes neuronal survival of septal cholinergic and dopaminergic neuronsSupported (in vitro)In vitroLow — single published study; cell culture only, no in vivo replication identified in source
Rescues neurons from glutamate-induced injurySupported (in vitro)In vitroLow — single published study; cell culture only, no in vivo replication identified in source
Neuroprotective effect in living organismsNot establishedIn vitroLow — no in vivo data present in source
Human therapeutic or neuroprotective applicationNot establishedNoneLow — no human evidence present in source

Assay conditions

This section reports conditions used in cell culture assays. It does not establish in vivo animal or human exposure.

ContextSystemAssay conditionTimepointEndpointLimitation
Cell culturePrimary cultures of neonatal rat septal cholinergic neuronsNot individually extracted from sourceNot individually extracted from sourceNeuronal survivalCell culture; no in vivo translation established
Cell culturePrimary cultures of neonatal rat mesencephalic dopaminergic neuronsNot individually extracted from sourceNot individually extracted from sourceNeuronal survivalCell culture; no in vivo translation established
Cell culturePrimary cultures of neonatal rat neuronsNot individually extracted from sourceNot individually extracted from sourceRescue from glutamate-induced injuryCell culture; no in vivo translation established

Assay limitations

  • All reported activity data derive from primary cell culture experiments; no in vivo animal or human data are identified.
  • The single published reference (Hama et al., 1996) is the sole attached evidence; independent replication is not documented.
  • The molecular target mediating neurotrophic activity is not specified in available literature.
  • In vitro neurotrophic activity does not establish systemic tolerability, in vivo efficacy, or clinical relevance.

Regulatory status

No approved therapeutic status identified. This card describes a research or literature-derived peptide, not an approved medicine.

Region / bodyStatusNotes
USNo approved statusper available sources; not independently verified in this card
EUNo approved statusper available sources; not independently verified in this card
WADANot checkedStatus not extracted from source; not independently verified in this card

Mechanism

BINP is proposed to act as a neurotrophic factor based on its isolated origin from traumatized rat brain tissue and its observed promotion of neuronal survival in primary cell cultures. activity toward septal cholinergic and mesencephalic dopaminergic neurons, consistent with a neurotrophic profile. The specific molecular target, receptor, or intracellular pathway has not been identified in available literature. This mechanism is inferred from cell culture observations and has not been validated in vivo.


Chemistry

FieldValue
Sequence (single-letter)EALELARGAIFQA
Full notationH-Glu-Ala-Leu-Glu-Leu-Ala-Arg-Gly-Ala-Ile-Phe-Gln-Ala-NH2
Length13 amino acids
TopologyLinear
C-terminal modificationAmide (–NH₂)
Molecular weightNot provided in source
FormulaNot provided in source
CASNot provided in source
Sequence confidenceNeeds review

Open questions

  • In vivo translation: No in vivo animal studies are documented. Whether the in vitro neurotrophic activity translates to living organisms has not been established.
  • Molecular target: The receptor or molecular mechanism underlying BINP's neurotrophic activity has not been identified in available literature.
  • Human relevance: No human evidence is present, whether any neuroprotective effect is translatable to human biology is unknown.
  • Replication: A single published study from 1996 is the sole attached evidence; independent replication studies are not documented.
  • Long-term stability and formulation: Published research provides only storage conditions; no pharmaceutical formulation or stability data beyond lyophilized form are present.
Hypotheses5 directions▾ collapse

Research directions for this peptide, selected from the current sources — hypotheses you can explore and model. None of it is proven yet; tap any one to see the full thinking.

openupdated 2026-06-05

Does BINP protect only certain brain cells because those cells carry the receptor it binds, rather than because of something special in the peptide's chemical makeup?

If receptor location controls which cells BINP protects, doctors could predict which patients and which brain diseases would respond to it just by looking at receptor maps from existing brain databases. That would make clinical trial design much faster and cheaper, and could help match the right patients to the treatment.

The hypothesis
BINP's neuroprotective selectivity for cholinergic and dopaminergic neurons over other neuron types is not intrinsic to the peptide sequence itself but is determined by the restricted expression pattern of NPBWR1 in the CNS, predicting that any tissue or tumor cell line forced to express NPBWR1 would become similarly responsive to BINP.
Why it’s plausible
The readme specifies that BINP benefits septal cholinergic and mesencephalic dopaminergic neurons specifically. These populations overlap substantially with the central distribution of NPBWR1/GPR7 expression reported in rodent brain. If NPBWR1 expression is the gating factor, then BINP's selectivity is pharmacological rather than structural: the peptide does not inherently discriminate cell types but is recruited wherever its receptor is expressed. This would also mean BINP would be ineffective in conditions where the relevant neurons down-regulate NPBWR1 (e.g., late-stage Parkinson's disease).
Why it matters
Receptor-expression-gated selectivity is a testable, predictive model that reframes BINP as a precision tool whose therapeutic scope can be read out from receptor expression atlases, including single-cell transcriptomic data.
Plausibility.40
Novelty.70
Impact.70
Basis · grounding3 computed/notes
[1]
noteSelective protection of septal cholinergic and mesencephalic dopaminergic neurons in culture
[2]
structureHigh-confidence NPBWR1 binding pose (ipTM=0.954) supports NPBWR1 as the selectivity-determining receptor
[3]
sequenceEALELARGAIFQA has no documented cell-type-specific uptake motif, arguing against intrinsic cell-type discrimination by the peptide alone
openupdated 2026-06-05

Does BINP work by switching on a known brain signaling receptor, rather than acting through a vague or unknown mechanism?

If true, doctors and researchers would have a precise molecular handle for developing BINP-based drugs, making it far easier to design better versions and predict which patients might benefit. It would move this peptide from a mysterious lab curiosity into a real drug development pipeline.

The hypothesis
BINP (EALELARGAIFQA) binds neuropeptide B/W receptor 1 (NPBWR1) with high affinity and acts as an agonist or partial agonist at this Gi-coupled GPCR, accounting for its neurotrophic activity in cholinergic and dopaminergic neurons.
Why it’s plausible
The Boltz-2 complex prediction yields an exceptionally high ipTM of 0.954, indicating a confident, well-packed binding pose with NPBWR1. NPBWR1 (GPR7) is expressed in limbic and striatal circuits that overlap precisely with the septal cholinergic and mesencephalic dopaminergic populations BINP protects in culture. Gi-coupled signaling downstream of NPBWR1 activates PI3K/Akt and MAPK/ERK cascades, both of which are canonical neuronal survival pathways. If BINP is a functional ligand at NPBWR1, the receptor rather than a generic membrane interaction is the mechanistic anchor for its neurotrophic effect.
Why it matters
Assigning BINP a specific GPCR target transforms it from an orphan neuropeptide fragment into a tractable lead for receptor-targeted neuroprotection, enabling structure-activity work grounded in a defined binding site.
Plausibility.35
Novelty.70
Impact.80
Basis · grounding3 computed/notes
[1]
structureBoltz-2 BINP/NPBWR1 complex ipTM=0.954, pLDDT=86.6, indicating high-confidence interface geometry
[2]
sequenceEALELARGAIFQA: amphipathic character with hydrophobic C-terminus (GAIFQA) consistent with GPCR transmembrane pocket insertion
[3]
noteBINP protects septal cholinergic and mesencephalic dopaminergic neurons, regions with documented NPBWR1 expression
openupdated 2026-06-05

Is the business end of BINP just its short hydrophobic tail, with the rest acting mainly as a handle?

If the active core is just six amino acids, chemists could build a much smaller, more drug-like molecule that does the same job, one that survives longer in the body and crosses into the brain more easily. Smaller peptides are generally cheaper to make and easier to turn into medicines.

The hypothesis
The hydrophobic C-terminal segment GAIFQA of BINP constitutes the core receptor-binding pharmacophore, while the N-terminal EALE segment provides solubility and helical stabilization that orientates the pharmacophore correctly, such that C-terminally truncated analogs lose receptor affinity but N-terminally truncated analogs retain or gain potency.
Why it’s plausible
Inspection of EALELARGAIFQA reveals two functional sub-regions: a negatively charged, helix-favoring N-terminus (EALE, Glu-Ala-Leu-Glu) and a compact hydrophobic C-terminus (GAIFQA, Gly-Ala-Ile-Phe-Gln-Ala). GPCR peptide ligands typically engage transmembrane binding pockets primarily through hydrophobic residues, with charged extensions serving as solubility or selectivity handles. The central Arg (position 7) may form an ionic contact with an acidic residue in the NPBWR1 extracellular loop. This architecture predicts a clear structure-activity relationship along the peptide length.
Why it matters
If the C-terminal pharmacophore hypothesis is correct, shorter, more metabolically stable analogs retaining GAIFQA could be designed with improved CNS penetration and reduced peptide bond lability.
Plausibility.45
Novelty.60
Impact.60
Basis · grounding2 computed/notes
[1]
sequenceEALELARGAIFQA: positions 1-4 (EALE) are charged/helix-forming; position 7 (Arg) is cationic; positions 8-13 (GAIFQA) are hydrophobic/compact
[2]
structureBoltz-2 pLDDT=86.6 indicates a well-ordered bound conformation, consistent with defined sub-region roles
openupdated 2026-06-05

Does BINP stop the chain reaction of cell death by quieting a GPCR relay, rather than physically blocking glutamate?

Current drugs that directly block glutamate can scramble perception and cognition. If BINP works through a more targeted relay, it might prevent stroke or traumatic brain injury damage without those mental side effects, a major unmet need in neurology.

The hypothesis
BINP suppresses glutamate excitotoxicity in part by reducing NMDA receptor overactivation downstream of NPBWR1-Gi signaling, rather than by direct glutamate receptor antagonism, such that its neuroprotective potency is dependent on ambient NPBWR1 receptor density and G-protein coupling efficiency in the target neuron.
Why it’s plausible
BINP was shown to rescue cultured neurons from glutamate-induced injury. Gi-coupled GPCRs, including NPBWR1, reduce cAMP and modulate calcium influx, which can dampen the membrane depolarization that sustains NMDA receptor overactivation during excitotoxic episodes. This predicts that the neuroprotective effect of BINP is cell-type-contingent: neurons expressing high NPBWR1 levels (septal cholinergic, dopaminergic) will be most protected, while neurons with low receptor expression will be largely unresponsive, explaining the cell-type selectivity already observed.
Why it matters
Establishing an indirect, receptor-gated mechanism for glutamate antagonism would distinguish BINP from conventional NMDA blockers (which cause psychotomimetic side effects) and position it as a selective, circuit-specific neuroprotectant.
Plausibility.40
Novelty.60
Impact.70
Basis · grounding3 computed/notes
[1]
noteBINP protects cultured neurons from glutamate-induced injury and promotes survival of specific cholinergic and dopaminergic neuron populations
[2]
structureHigh-confidence NPBWR1 complex (ipTM=0.954) supports a receptor-mediated rather than membrane-disruptive mechanism
[3]
sequence13-aa linear peptide is too small to span a lipid bilayer or form an ion-channel pore, making direct membrane/receptor channel blockade unlikely
openupdated 2026-06-05

Is BINP something the damaged brain already releases to protect itself, and could giving more of it improve recovery?

If BINP is a natural distress signal the brain already uses, boosting its levels after a head injury or stroke could amplify the brain's own healing response. That would be a fundamentally safer starting point than most current experimental treatments, which introduce entirely foreign chemicals.

The hypothesis
BINP holds therapeutic potential for acute neurotrauma (traumatic brain injury, perinatal hypoxia-ischemia) because it was isolated from injured brain tissue and is presumably released endogenously as a damage-response signal, implying its natural concentration at injury sites is self-limiting and its pharmacological dosing window is therefore defined by endogenous titration rather than arbitrary toxicity thresholds.
Why it’s plausible
BINP was isolated from traumatized rat brain, suggesting it is either cleaved from a larger precursor or up-regulated in response to neuronal stress. Endogenous peptides released at injury sites often act in a paracrine neuroprotective loop (analogous to BDNF, VGF-derived peptides). If BINP is such a damage-response mediator, therapeutic administration would amplify an already-initiated protective program rather than introduce a foreign pharmacology, which historically correlates with better tolerability and dose predictability in neuropeptide clinical translation.
Why it matters
Framing BINP as an endogenous protective mediator rather than a synthetic drug provides a mechanistic rationale for its use in the acute injury window and a natural pharmacokinetic precedent for dosing.
Plausibility.55
Novelty.30
Impact.50
Basis · grounding2 computed/notes
[1]
noteBINP was originally isolated from traumatized rat brain tissue, implying endogenous production under injury conditions
[2]
notePromotes survival of septal cholinergic and mesencephalic dopaminergic neurons in vitro, two populations heavily damaged in TBI and ischemia
details expand to inspect
full evidence table2 metrics
metricvaluetool
ipTM 0.9538408517837524 boltz-2
ranking score 0.8833171725273132 boltz-2
3-letter notation
Glu-Ala-Leu-Glu-Leu-Ala-Arg-Gly-Ala-Ile-Phe-Gln-Ala
recipeboltz-2 2.2.1
parametervalue
modelboltz-2 2.2.1
weights
hardwarevast_v100_32gb
mlx version
python
random seed1
msa strategycolabfold_local
runtime
predicted by
predicted at2026-05-22
citationbibtex
peptidemodel (2026). Brain-protective peptide found in injured rat brain (BINP) (pep-10530, v1). PeptideModel. https://peptidemodel.com/card/pep-10530
@peptide{pep10530,
  sequence = {EALELARGAIFQA},
  target   = {npbwr1},
  author   = {peptidemodel},
  year     = {2026},
  status   = {computed}
}
clinical trials 15 on ct.gov · checked 2026-05-09
ct.gov trials 15
with results 1
by phase
1phase 11phase 21phase 31phase 47no phase
by status
3completed2active3not yet recruiting1unknown
references 4 papers
discussion no comments
sign in to comment
peptidemodel.com CC-BY-SA-4.0 research only · not for human use