PAL-KTTKS is a palmitoylated pentapeptide composed of the sequence Lys-Thr-Thr-Lys-Ser (KTTKS) linked to an N-terminal C16 palmitoyl group. The KTTKS sequence originates from the carboxyl-terminal propeptide region of type I procollagen and has been studied as a matrix-derived signaling sequence associated with extracellular-matrix regulation.
The addition of the lipid chain converts the hydrophilic KTTKS sequence into an amphiphilic lipopeptide, making PAL-KTTKS particularly useful for research involving peptide lipidation, fibroblast biology, matrix remodeling, formulation, and structure–activity relationships.
Product Information
| Property | Specification |
|---|---|
| Product Name | PAL-KTTKS |
| Catalog No. | AS2808 |
| Sequence | Pal-Lys-Thr-Thr-Lys-Ser |
| Short Form | Pal-KTTKS |
| Peptide Length | 5 amino acids |
| Lipid Modification | N-terminal palmitoyl group |
| Lipid Chain | C16 |
| Purity | Crude to 98% |
| Peptide Class | Lipidated matrix-derived peptide |
| Research Areas | ECM biology, fibroblasts, peptide lipidation, collagen-related research |
KTTKS Sequence and Matrix Origin
The peptide portion of PAL-KTTKS is:
Lys-Thr-Thr-Lys-Ser
KTTKS represents a short sequence associated with the C-terminal propeptide of type I procollagen. It has been investigated as a matrikine-related signal capable of influencing extracellular-matrix responses in fibroblast systems.
This molecular origin is important for research interpretation. KTTKS is not a laminin-derived integrin-binding motif, and PAL-KTTKS should not be described as a laminin peptide.
Instead, its principal research context is the relationship between a procollagen-derived signaling sequence and extracellular-matrix homeostasis.
Why PAL-KTTKS Is Lipidated
The N-terminus of KTTKS is modified with a C16 palmitoyl chain.
Unmodified KTTKS is relatively hydrophilic. Palmitoylation increases hydrophobic character and creates an amphiphilic molecule containing both a peptide domain and a fatty-acid domain.
This modification can influence membrane association, formulation behavior, chromatographic retention, physical stability, and distribution within experimental systems. Studies comparing KTTKS with its palmitoylated derivative therefore provide a useful model for understanding how lipid conjugation changes peptide behavior.
Researchers investigating alternative fatty-acid chains, linker strategies, or KTTKS analogs can explore our Custom Peptide Synthesis capabilities.
Extracellular Matrix Research
KTTKS and PAL-KTTKS have been studied in fibroblast models in relation to extracellular-matrix production, including collagen- and fibronectin-associated responses.
For experimental design, we consider it more accurate to describe PAL-KTTKS as a lipidated matrix-signaling peptide rather than simply a short collagen fragment. The biological question is not whether the molecule becomes structural collagen, but how cells respond to the matrix-derived sequence.
The lipid modification introduces an additional variable that may alter exposure of the peptide sequence to cells and membranes.
Amphiphilic Behavior and Formulation
PAL-KTTKS differs substantially from a conventional unmodified pentapeptide because the C16 chain increases hydrophobicity.
Depending on concentration and solvent conditions, lipidated peptides may display aggregation or self-association behavior that affects apparent solubility and experimental delivery. A clear solution at one concentration does not necessarily predict identical behavior after dilution into an aqueous assay system.
Laboratories should therefore document solvent composition, concentration, mixing conditions, and final assay medium when comparing PAL-KTTKS data.
Research Applications
PAL-KTTKS is suited to studies involving extracellular-matrix signaling, fibroblast responses, collagen-related pathways, peptide amphiphiles, lipidated peptide design, formulation research, and skin-remodeling models.
It is also a useful reference molecule for comparing KTTKS versus lipidated KTTKS, or for examining how changes in fatty-acid chain length influence physicochemical and biological behavior.
Synthetic and Quality Control Considerations
Palmitoylation changes both synthesis and purification behavior. The fatty-acid chain increases hydrophobicity and can shift RP-HPLC retention relative to the unmodified peptide.
Final material should therefore be evaluated as the complete lipidated molecule rather than as the KTTKS backbone alone. Analytical HPLC and mass spectrometry support evaluation of chromatographic purity and expected molecular mass.
Our Peptide Quality Control resources provide additional information on HPLC, MS, solubility, and project-specific analytical documentation.
Purity and Experimental Planning
The appropriate purity depends on the downstream study. Exploratory formulation or physicochemical work may have different requirements from quantitative fibroblast or cell-based assays.
Researchers can review our Recommended Peptide Purity guidance when selecting a specification.
For PAL-KTTKS projects, We recommend confirming the KTTKS sequence, palmitoylation state, expected molecular mass, purity, and intended solvent system before experimental work begins.
Frequently Asked Questions
What is PAL-KTTKS?
PAL-KTTKS is a five-amino-acid KTTKS peptide carrying an N-terminal C16 palmitoyl group. It is also widely referred to as palmitoyl pentapeptide-4.
Where does the KTTKS sequence come from?
KTTKS is associated with a short region of the carboxyl-terminal propeptide of type I procollagen and has been studied as a matrix-derived signaling sequence.
Is PAL-KTTKS derived from laminin?
No. KTTKS is associated with type I procollagen, not the γ1 chain of laminin. These are biologically distinct extracellular-matrix proteins.
Why is KTTKS palmitoylated?
The lipid modification increases hydrophobicity and changes the physicochemical properties of the peptide. This can influence formulation, membrane association, stability, and delivery behavior.
Is PAL-KTTKS identical to every commercial Matrixyl formulation?
PAL-KTTKS is the defined peptide commonly referred to as palmitoyl pentapeptide-4. Commercial ingredient formulations may contain solvents, carriers, stabilizers, or other components and should not automatically be treated as equivalent to isolated research-grade peptide.
Can alternative lipidated KTTKS analogs be synthesized?
Yes. Fatty-acid chain length, sequence substitutions, terminal chemistry, purity, and quantity can be evaluated according to the intended research design.
Research Use Only.