Regenerative · Extracellular matrix-derived adhesion motif
Laminin-derived peptide IKVAV
Also known as Ile-Lys-Val-Ala-Val
A laminin α1-derived pentapeptide studied as a presentation-dependent cue in neural cell cultures and engineered matrices.
- Length
- 5 amino acids
- Half-life
- Not well characterised
- Mechanism
- IKVAV is a laminin α1-chain motif associated with cell adhesion and neurite extension in experimental systems. Its activity depends strongly on presentation; integrin-associated signalling has been implicated, but the isolated pentapeptide does not have one universally established receptor target.
- Studied in
- Neuronal cultures, neural progenitor models and peptide-functionalised scaffolds are used to examine IKVAV-dependent adhesion, neurite morphology and cell–matrix signalling.
About Laminin-derived peptide IKVAV
IKVAV consists of isoleucine, lysine, valine, alanine and valine. It was identified through synthetic peptide mapping of the laminin A chain, now termed the α1 chain, within a region associated with cell attachment and neurite-promoting activity. The five-residue sequence represents a small fragment of a much larger extracellular matrix protein. An isolated IKVAV peptide therefore reproduces neither the full architecture nor all receptor-binding properties of native laminin.
Experimental platforms frequently display IKVAV on hydrogels, fibres or self-assembling peptide constructs rather than study only the freely soluble sequence. These formats can alter ligand accessibility, local density and mechanical context, each of which influences cellular responses. Integrin-associated adhesion pathways are relevant, although receptor attribution varies with the cell type and material. Research commonly measures neurite length, attachment, differentiation markers and scaffold organisation, with suitable controls for the underlying material.
Laboratory notes
- Specify terminal chemistry, purity and any linker or conjugation handle; modified IKVAV constructs are not chemically equivalent to the free pentapeptide.
- For surface assays, quantify accessible ligand density and include an unmodified material and a composition-matched scrambled-sequence control.
- Follow lot-specific solubility guidance, prepare aliquots where appropriate and monitor aggregation or adsorption that could change the available peptide concentration.
Storage and reconstitution basics: storage guide.
Questions about Laminin-derived peptide IKVAV
Is IKVAV a complete laminin substitute?
No. It is one short laminin-derived motif and lacks the multidomain structure, additional binding sites and assembly properties of the parent protein.
Does IKVAV have a single established receptor?
A single receptor assignment is not established across experimental systems. Integrin-associated mechanisms have been reported, but receptor-blocking or genetic experiments are needed in the specific model.
Why can soluble and scaffold-bound IKVAV give different results?
Immobilisation changes ligand density, orientation and clustering, while the scaffold adds mechanical and structural cues absent from a soluble-peptide assay.
Is Laminin-derived peptide IKVAV for human use?
No. It is supplied strictly for in-vitro laboratory research and is not for human or animal consumption.
Related research peptides
All products are sold for laboratory research use only. Not for human consumption, not a medicine, not for diagnosing, treating or preventing any condition.