RecruitingPhase 4NCT07255248
Hoffa's Fat Pad Impingement (HFPI)
Boston Children's Hospitaln = 621 Mar 2026 to est. 2 Jan 2028
Hoffa's Fat Pad Impingement
Octreotide / Studies
Synthetic analog · 8 amino acids · 1,019.2 Da
Octreotide studies and research data
PepBank has 134 octreotide studies with results. All of them gave octreotide, with 816 results, grouped by what the studies measured. In each group, results from studies in people come first. Data as of 2026-10-30.
Searches 816 results and 2,448 papers. Newer studies from Europe PMC
Results in people
711
87% of 816 results
Results in animals
105
13% of 816 results
Results in lab cells
0
0% of 816 results
From computer models
0
0% of 816 results
The molecule
Octreotide identity
Identifiers, parent molecule, targets and development stage, from curated data.
Octreotide is a cyclic eight-residue somatostatin analog. The short-acting injection, depot products, and oral products have different regimens. Radiolabeled derivatives are separate substances.
- Kind
- Synthetic analog · 8 residues
- Identifiers
- ChEMBLCHEMBL1680 (opens in a new tab)PubChem CID448601 (opens in a new tab)UNIIRWM8CCW8GP (opens in a new tab)DrugBankDB00104 (opens in a new tab)CAS83150-76-9
- Parent
- Analog of SomatostatinOctreotide is a synthetic somatostatin analog. P61278 identifies the human somatostatin precursor, not octreotide. No contiguous parent interval is assigned.
- Development
- Approved in the US and EU (Sandostatin)An approved medicinal product exists. Availability and other indications can differ. Source (opens in a new tab)
Targets
| Target | Action | Evidence |
|---|---|---|
| Somatostatin receptors | Agonist | IUPHAR/BPS Guide to PHARMACOLOGY records human SST2, SST3, and SST5 receptor agonism.Source (opens in a new tab) |
Sequence and structure
Residues, differences from the parent, calculated properties and 3D structure. Source values and calculated values are shown separately.
Sequence
8 amino acids · 3 modifications · 1 disulfide bond
H-
Residues 1 to 8:
CFKTC
Parent: Somatostatin
No sequence is listed for the parent, so no alignment is shown.Octreotide is a synthetic somatostatin analog. P61278 identifies the human somatostatin precursor, not octreotide. No contiguous parent interval is assigned.
Properties
From identity sources
- Formula
- C49H66N10O10S2
- Molecular weight
- 1,019.2 g/mol
- Monoisotopic mass
- 1,018.4405 Da
- GSRS UNII RWM8CCW8GP(opens in a new tab)retrieved 2026-10-27
- PubChem CID 448601(opens in a new tab)retrieved 2026-10-27
- Curated Sandostatin US label(opens in a new tab)retrieved 2026-10-27
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)
- 0.550
- Mean Kyte-Doolittle hydropathy · Kyte and Doolittle 1982
- Positive: hydrophobic on average.
- Extinction coefficient, 280 nm (Cys reduced)
- 5,500 M⁻¹ cm⁻¹
- 5500 x Trp + 1490 x Tyr · Pace et al. 1995 (ExPASy ProtParam)
- Extinction coefficient, 280 nm (all Cys as cystines)
- 5,625 M⁻¹ cm⁻¹
- 5500 x Trp + 1490 x Tyr + 125 x cystine · Pace et al. 1995 (ExPASy ProtParam)
- Instability index
- 49.50
- Dipeptide instability weights (DIWV) · Guruprasad et al. 1990
- Above 40: classed as possibly unstable (ExPASy).
- Aliphatic index
- 0.0
- Mole % A + 2.9 V + 3.9 (I + L) · Ikai 1980
- Boman index
- −0.02 kcal/mol
- Mean solubility value (negated) · Boman 2003
- 2.48 or below: lower protein-binding potential (Boman).
- Hydrophobic moment (μH)
- Not calculated
- The sequence is too short for this method.
- Not included: other modification. Mass, charge and pI are not calculated; use the identity-source values.
- The C-terminal group is not modeled.
- D-amino acids have the same mass and charge as L forms. Hydrophobicity scales were measured on L forms.
- 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
- Aromatic38% (3)F W
- Positive13% (1)K
- Polar25% (2)T
- Special25% (2)C
8 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 Phe2 · 25%
W Trp1 · 13%
Y Tyr0 · 0%
H His0 · 0%
K Lys1 · 13%
R Arg0 · 0%
D Asp0 · 0%
E Glu0 · 0%
N Asn0 · 0%
Q Gln0 · 0%
S Ser0 · 0%
T Thr2 · 25%
C Cys2 · 25%
G Gly0 · 0%
P Pro0 · 0%
3D structure
PredictedAlphaFold DB · P61278
Loads the 3D viewer (3Dmol.js, about 150 KB) and the model file from AlphaFold DB (EMBL-EBI).
2D structure
Draws the structure in your browser with RDKit (about 2.3 MB, loaded once).
SMILES fromPubChem CID 448601(opens in a new tab)
C[C@H]([C@H]1C(=O)N[C@@H](CSSC[C@@H](C(=O)N[C@H](C(=O)N[C@@H](C(=O)N[C@H](C(=O)N1)CCCCN)CC2=CNC3=CC=CC=C32)CC4=CC=CC=C4)NC(=O)[C@@H](CC5=CC=CC=C5)N)C(=O)N[C@H](CO)[C@@H](C)O)OResults 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
Newer studies
PepBank reads each paper before it shows the results. This search looks in Europe PMC for newer papers that PepBank has not read yet.
Status and safety
Data