Cathelicidin antimicrobial peptide precursor (hCAP18) studies and research data
PepBank has no study results for Cathelicidin antimicrobial peptide precursor (hCAP18) yet. Data as of 2026-10-30.
Searches 0 results and 0 papers. Newer studies from Europe PMC
Cathelicidin antimicrobial peptide precursor (hCAP18) identity
Identifiers, parent molecule, targets and development stage, from curated data.
hCAP18 is the 18 kDa cathelicidin precursor encoded by CAMP (UniProt P49913; 170 residues including a 30-residue signal peptide). It has an N-terminal cathelin-like domain (31-131) and a C-terminal antimicrobial region. Proteinase 3 cleaves it to release LL-37 (134-170); on skin, a serine protease-dependent process in sweat produces shorter peptides such as KR-20, KS-30 and RK-31. UniProt reports expression in neutrophilic granulocytes and bone marrow.
- Kind
- Natural peptide · 170 residues
- Identifiers
- UniProtP49913 (opens in a new tab)PDB4EYC (opens in a new tab)
- Development
- No known clinical developmentNo development of the precursor itself found. The derived peptide LL-37 (ropocamptide) reached phase 2. Source (opens in a new tab)
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
170 amino acids · 2 modifications · 2 disulfide bonds
Properties
From identity sources
No formula or molecular weight is listed for Cathelicidin antimicrobial peptide precursor (hCAP18).
Calculated from the sequence
Some values cannot be calculated. A terminal group is not modeled here.
- Average mass
- Not calculated
- Monoisotopic mass
- Not calculated
- Isoelectric point (pI)
- Not calculated
- Net charge at pH 7.4
- Not calculated
- GRAVY (hydropathy)
- −0.442
- Mean Kyte-Doolittle hydropathy · Kyte and Doolittle 1982
- Negative: hydrophilic on average.
- Extinction coefficient, 280 nm (Cys reduced)
- 8,480 M⁻¹ cm⁻¹
- 5500 x Trp + 1490 x Tyr · Pace et al. 1995 (ExPASy ProtParam)
- Extinction coefficient, 280 nm (all Cys as cystines)
- 8,730 M⁻¹ cm⁻¹
- 5500 x Trp + 1490 x Tyr + 125 x cystine · Pace et al. 1995 (ExPASy ProtParam)
- Instability index
- 37.59
- Dipeptide instability weights (DIWV) · Guruprasad et al. 1990
- 40 or below: classed as stable (ExPASy).
- Aliphatic index
- 87.1
- Mole % A + 2.9 V + 3.9 (I + L) · Ikai 1980
- Boman index
- 2.25 kcal/mol
- Mean solubility value (negated) · Boman 2003
- 2.48 or below: lower protein-binding potential (Boman).
- Hydrophobic moment (μH)
- 0.966
- Eisenberg scale, 100° per residue, best 11-residue window · Eisenberg et al. 1982, 1984
- 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 terminal group is not modeled here.
Composition
- Hydrophobic29% (50)A I L M V
- Aromatic6% (11)F W Y
- Positive18% (31)H K R
- Negative13% (22)D E
- Polar19% (33)N Q S T
- Special14% (23)C G P
170 residues. Each residue counts in one class; F and W count as aromatic.
3D structure
Loads the 3D viewer (3Dmol.js, about 150 KB) and the model file from RCSB PDB.
Helical wheel
An ideal alpha-helix projection. It shows where the hydrophobic residues fall if the peptide folds as a helix. It does not show that it does.
- μH, residues shown
- 0.242
- μH, best 11-residue window
- 0.966
- Arrow direction
- 221°
- Residues
- 1–54 of 170 · 3 rings of 18
Eisenberg consensus (normalized) scale · + K, R · − D, E
Assumes an ideal α-helix: 100° per residue, 3.6 residues per turn. The arrow is the mean hydrophobic moment (Eisenberg et al. 1984) and points at the hydrophobic face.
Show as table
| Position | Residue | Angle | Eisenberg consensus (normalized) |
|---|---|---|---|
| 1 | M | 0° | 0.64 |
| 2 | K | 100° | -1.50 |
| 3 | T | 200° | -0.05 |
| 4 | Q | 300° | -0.85 |
| 5 | R | 40° | -2.53 |
| 6 | D | 140° | -0.90 |
| 7 | G | 240° | 0.48 |
| 8 | H | 340° | -0.40 |
| 9 | S | 80° | -0.18 |
| 10 | L | 180° | 1.06 |
| 11 | G | 280° | 0.48 |
| 12 | R | 20° | -2.53 |
| 13 | W | 120° | 0.81 |
| 14 | S | 220° | -0.18 |
| 15 | L | 320° | 1.06 |
| 16 | V | 60° | 1.08 |
| 17 | L | 160° | 1.06 |
| 18 | L | 260° | 1.06 |
| 19 | L | 0° | 1.06 |
| 20 | L | 100° | 1.06 |
| 21 | G | 200° | 0.48 |
| 22 | L | 300° | 1.06 |
| 23 | V | 40° | 1.08 |
| 24 | M | 140° | 0.64 |
| 25 | P | 240° | 0.12 |
| 26 | L | 340° | 1.06 |
| 27 | A | 80° | 0.62 |
| 28 | I | 180° | 1.38 |
| 29 | I | 280° | 1.38 |
| 30 | A | 20° | 0.62 |
| 31 | Q | 120° | -0.85 |
| 32 | V | 220° | 1.08 |
| 33 | L | 320° | 1.06 |
| 34 | S | 60° | -0.18 |
| 35 | Y | 160° | 0.26 |
| 36 | K | 260° | -1.50 |
| 37 | E | 0° | -0.74 |
| 38 | A | 100° | 0.62 |
| 39 | V | 200° | 1.08 |
| 40 | L | 300° | 1.06 |
| 41 | R | 40° | -2.53 |
| 42 | A | 140° | 0.62 |
| 43 | I | 240° | 1.38 |
| 44 | D | 340° | -0.90 |
| 45 | G | 80° | 0.48 |
| 46 | I | 180° | 1.38 |
| 47 | N | 280° | -0.78 |
| 48 | Q | 20° | -0.85 |
| 49 | R | 120° | -2.53 |
| 50 | S | 220° | -0.18 |
| 51 | S | 320° | -0.18 |
| 52 | D | 60° | -0.90 |
| 53 | A | 160° | 0.62 |
| 54 | N | 260° | -0.78 |
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.
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.
Cathelicidin antimicrobial peptide precursor (hCAP18) studies: 0 papers with results
No paper with results is linked to this peptide.