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Matrixyl (palmitoyl pentapeptide-4) / Studies
Synthetic analog · 5 amino acids · 802.1 Da

Matrixyl (palmitoyl pentapeptide-4) studies and research data

PepBank has 23 Matrixyl studies with results. 11 of them gave Matrixyl, with 26 results, grouped by what the studies measured. In each group, results from studies in people come first. Data as of 2026-10-30.

Searches 26 results and 35 papers. Newer studies from Europe PMC

Results in people
6
23% of 26 results
Results in animals
10
38% of 26 results
Results in lab cells
10
38% of 26 results
From computer models
0
0% of 26 results
The molecule

Matrixyl identity

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

Original Matrixyl is Pal-KTTKS, with an N-terminal palmitoyl group and a free C-terminal acid. Its unlipidated parent is Pentapeptide-4 (KTTKS). Matrixyl 3000 contains Pal-GHK and Pal-GQPR. Matrixyl Synthe-6 contains a different peptide. Exact natural precursor mapping remains unconfirmed.

Kind
Synthetic analog · 5 residues
Identifiers
PubChem CID9897237 (opens in a new tab)UNIIKK181SM5JG (opens in a new tab)CAS214047-00-4
Parent
Modified form of Pentapeptide-4 (KTTKS)Palmitoylation attaches a C16 fatty-acid group to the N terminus of KTTKS. CIR describes KTTKS as a type I procollagen subfragment. Exact protein accession and coordinates remain unconfirmed.
Development
UnknownA formal clinical development phase was not established.

Targets

No molecular target is recorded for this peptide.

Sequence and structure

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

Sequence

5 amino acids · 1 modification

Residues 1 to 5:
TTKS
-OH
  • PositiveK R H
  • PolarS T N Q
  • Modified residue

Modifications

1
Lipidation
N-terminal palmitoyl (C16) group.

Parent: Pentapeptide-4 (KTTKS)

No sequence is listed for the parent, so no alignment is shown.Palmitoylation attaches a C16 fatty-acid group to the N terminus of KTTKS. CIR describes KTTKS as a type I procollagen subfragment. Exact protein accession and coordinates remain unconfirmed.

Properties

From identity sources

Formula
C39H75N7O10
Molecular weight
802.1 g/mol
Monoisotopic mass
801.5575 Da

Calculated from the sequence

Some values cannot be calculated. A modification changes this value and is not modeled here (for example a lipid, metal or linker).

Average mass
Not calculated
Monoisotopic mass
Not calculated
Isoelectric point (pI)
Not calculated
Net charge at pH 7.4
Not calculated
GRAVY (hydropathy)
−2.000
Mean Kyte-Doolittle hydropathy · Kyte and Doolittle 1982
Negative: hydrophilic 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
8.00
Dipeptide instability weights (DIWV) · Guruprasad et al. 1990
40 or below: classed as stable (ExPASy).
Aliphatic index
0.0
Mole % A + 2.9 V + 3.9 (I + L) · Ikai 1980
Boman index
3.93 kcal/mol
Mean solubility value (negated) · Boman 2003
Above 2.48: high protein-binding potential (Boman).
Hydrophobic moment (μH)
Not calculated
The sequence is too short for this method.
  • Not included: lipid chain. Mass, charge and pI are not calculated; use the identity-source values.
  • The N-terminal group is not modeled.
  • 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

No charge curve

A modification changes this value and is not modeled here (for example a lipid, metal or linker).

Composition

  • Positive40% (2)
  • Polar60% (3)

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

A Ala0 · 0%
I Ile0 · 0%
L Leu0 · 0%
M Met0 · 0%
V Val0 · 0%
F Phe0 · 0%
W Trp0 · 0%
Y Tyr0 · 0%
H His0 · 0%
K Lys2 · 40%
R Arg0 · 0%
D Asp0 · 0%
E Glu0 · 0%
N Asn0 · 0%
Q Gln0 · 0%
S Ser1 · 20%
T Thr2 · 40%
C Cys0 · 0%
G Gly0 · 0%
P Pro0 · 0%

3D structure

No 3D structure

No experimental structure (PDB) and no UniProt entry for an AlphaFold model are listed for this peptide. Synthetic peptides often have neither. The sequence view above is the reference.

2D structure

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

SMILES fromPubChem CID 9897237(opens in a new tab)

CCCCCCCCCCCCCCCC(=O)N[C@@H](CCCCN)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H]([C@@H](C)O)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CO)C(=O)O
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