NAP and D-SAL: neuroprotection against the beta amyloid peptide (1-42).

Gozes I, Divinski I, Piltzer I

BMC neuroscience10 Dec 2008Cited by 43 (Europe PMC)

PMID19091000PMCIDPMC2604881DOI10.1186/1471-2202-9-s3-s3PepBankPUB-19091000

Summary

IntroductionNAP (Asn-Ala-Pro-Val-Ser-Ile-Pro-Gln, single amino acid letter code, NAPVSIPQ), an eight amino acid neuroprotective peptide derived from activity-dependent neuroprotective protein (ADNP), exhibits some structural similarity to activity-dependent neurotropic factor-9 (ADNF-9; Ser-Alal-Leu-Leu-Arg-Ser-Ile-Pro-Ala, SALLRSIPA). Both peptides are also active in the all D-amino acid conformation, termed D-NAP and D-SAL. Original results utilizing affinity chromatography coupled to mass spectrometry identified tubulin, the subunit protein of microtubules, as the major NAP-associating protein in brain. The NAP-tubulin association was found to be diminished in the presence of ADNF-9, D-NAP, and D-SAL, suggesting a common target of neuroprotection. The beta amyloid peptide interacts with microtubules, and previous studies have demonstrated protection against beta amyloid (25-35) toxicity by NAP and ADNF-9. NAP also inhibits beta amyloid (25-35 and 1-40) aggregation.MethodsCerebral cortical cultures derived from newborn rats were used in neuronal survival assays to test the activity of both NAP and D-SAL against the major Alzheimer's disease toxic peptide beta amyloid (1-42).ResultsNAP and D-SAL protected cerebral cortical neurons against the major Alzheimer's disease toxic peptide beta amyloid (1-42). Maximal protection of both peptides was observed at concentrations of 10-15 to 10-10 mol/l.ConclusionThese findings, together with those of previous in vivo studies conducted in relevant Alzheimer's disease models, pave the path to drug development. Bioavailability studies indicated that NAP penetrates cells and crosses the blood-brain barrier after nasal or systemic administration. Phase II clinical trials of NAP are currently in progress by Allon Therapeutics Inc.

CC BYText from Europe PMC. Highlighted sentences are the source of results.

Results from this study1

1 result from studies that gave the peptide. No result from this study comes from people.

01LabIn vitro (cells)Efficacy outcome
In newborn rat cortical cultures, NAP protected neurons against beta amyloid toxicity, with maximal protection at the reported concentration range.
In plain wordsIn cells from newborn rats, NAP protected neurons against beta amyloid toxicity.
Peptide
Davunetide
Outcome
IncreaseNeuronal survival
Study
Ratn: not reported in source
Newborn rat cerebral cortical neuron cultures exposed to beta amyloid (1-42)
Outcome group
Neuroprotection · Nervous system and cognition
Studied dose
10-15 to 10-10 mol/lAs given in this study (Rat).
Source sentences
Summary
NAP and D-SAL protected cerebral cortical neurons against the major Alzheimer's disease toxic peptide beta amyloid (1-42).
2 context sentences(design, population, supporting numbers)
Summary · context
Maximal protection of both peptides was observed at concentrations of 10-15 to 10-10 mol/l.
Summary · context
Cerebral cortical cultures derived from newborn rats were used in neuronal survival assays to test the activity of both NAP and D-SAL against the major Alzheimer's disease toxic peptide beta amyloid (1-42).
Show in the study text Report a problemFND-1909100001

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Registered trials1

Trials this study reports on, or that list this study as a reference. Registry data from ClinicalTrials.gov.

1 trial · 1 completed · source ClinicalTrials.gov (opens in a new tab)

CompletedPhase 1NCT01056965

Davunetide (AL-108) in Predicted Tauopathies - Pilot Study

University of California, San Franciscon = 12Jan 2010 to Dec 2012

Predicted Tauopathies, Including · Progressive Supranuclear Palsy · Frontotemporal Dementia With Parkinsonism Linked to Chromosome 17 · Corticobasal Degeneration Syndrome · Progressive Nonfluent Aphasia

Trial page ClinicalTrials.govUpdated 5 Apr 2019

Version history

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Version 2Current
27 Oct 2026, 18:20 UTC
Study results updated
Version 1
27 Oct 2026, 16:32 UTC
First added · source update from Europe PMC

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