Record in detail
General Info
- lamp_id:L01A000628
- Name:PHYL2_PHYHY
- FullName:Phylloseptin-2
- Source:Phyllomedusa hypochondrialis
- Mass:2016.3 Da
- Sequence Length:19 aa
- Isoelectric Point:9.69
- Activity:Antibacterial
- Sequence
FLSLIPHAINAVSAIAKHN - Function:Has antimicrobial activity. No hemolytic activity.
Cross-Linking
- Cross-linking
- 1 Database:APD 546
- 2 Database:CAMP CAMPSQ588
- 3 Database:DBAASP 1652
- 4 Database:dbAMP dbAMP_02202
- 5 Database:DRAMP DRAMP01301
- 6 Database:SATPdb satpdb11891
- 7 Database:Uniprot P84567
Top similar AMPs
- Top similar AMPs on LAMP
- 1. L12A06189| From 47 To 64 E-value: 0.00001 Score: 40
FLSLIPHAINAVSAIAKH - 2. L12A06190| From 47 To 64 E-value: 0.00003 Score: 38.9
FLSLIPHAINAVSAIAKH - 3. L12A02203| From 1 To 19 E-value: 0.00003 Score: 38.5
FLSLIPHAINAVSAIAKHN - 4. L01A000628 From 1 To 19 E-value: 0.00003 Score: 38.5
FLSLIPHAINAVSAIAKHN - 5. L01A000630 From 1 To 19 E-value: 0.0001 Score: 37
FLSLIPHAINAVSAIAKHS
Activity
- Antibacterial Activities
- 1 Target: S.aureus MIC: 15.93 μg/ml (7.90061 μM)
- 2 Target: E.faecalis MIC: 8.07 μg/ml (4.00238 μM)
- 3 Target: E.coli MIC: 15.93 μg/ml (7.90061 μM)
- 4 Target: P.aeruginosa MIC: 8.07 μg/ml (4.00238 μM)
- 5 Target: E. coli MIC: 15.9288 μg/ml (7.9 μM)
- 6 Target: S. aureus MIC: 15.9288 μg/ml (7.9 μM)
Toxicity
- Toxicity
No toxicity records found on LAMP database
Reference
- Reference
- [1] Brand G.D.,Prates M.V.,Rodrigues M.I.S.,Silva L.P.,Leite J.R.S.A.,
- Title:Phylloseptins: a novel class of anti-bacterial and anti-protozoan peptides from the Phyllomedusa genus.
- Journal:Peptides, 2005, 26, 565-573 [PubMed:15752569]
- [2] Shaw C.,Walker B.,Gagliardo R.,Zhou M.,Chen T.,
- Title:Elements of the granular gland peptidome and transcriptome persist in air-dried skin of the South American orange-legged leaf frog, Phyllomedusa hypocondrialis.
- Journal:Peptides, 2006, 27, 2129-2136 [PubMed:16713656]
- [3] Almeida F.C.,Cesar A.,Prates M.V.,Moraes C.M.,Resende J.M.,
- Title:Solution NMR structures of the antimicrobial peptides phylloseptin-1, -2, and -3 and biological activity: the role of charges and hydrogen bonding interactions in stabilizing helix conformations.
- Journal:Peptides, 2008, 29, 1633-1644 [PubMed:18656510]
Comments
- Comments
No comments found on LAMP database