‹ ›
MYP_156318
← PREVIOUS NEXT → BACK
Basic Information
H3A/H4A
Antimicrobial
Antimicrobial ▸ Antibacterial
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-negative
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-positive
Antimicrobial ▸ Antifungal
Toxicity / Safety ▸ Blood cell toxicity ▸ Hemolysis ▸ Hemolytic
Standard
25 amino acids
C129H222N46O27
Standard
Sequence
FIAAIIGGLFSAGKAIHRLIRRRRR
Physicochemical Analysis
2849.43 Da
12.00
6.85
6.59
0.2738
0.27
0.97
-0.08
107.72
125.20
0.0800
0.00
0.00
The radar chart summarizes major physicochemical dimensions for quick comparison, while exact numerical values remain listed on the left.
Residue Composition
Amino Acid Composition
Chemical Descriptors
1208.05
-9.52
47.0
35.0
98.0
202.0
3.0
24.0
Structural Visualization
3D PDB MODEL
Drag to rotate. Click a residue or atom to inspect it; the selected residue is highlighted in amber in the current view mode. Use the buttons to zoom.
2D CHEMICAL STRUCTURE
Drag to move
Drag to move. Use the buttons to zoom.
Experimental Records
RECORD: Rec_0237490 VERIFIED: YES
Provenance & Taxonomy
Synthetic construct [Synthetic]
32630
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
None
Bio-Activity Profile
Antimicrobial Antibacterial Anti-Gram-positive Antifungal
PaperHydrophobic residues are critical for the helix-forming, hemolytic and bactericidal activities of amphipathic antimicrobial peptide TP4. PLoS One. 2017 Oct 17;12(10):e0186442. doi: 10.1371/journal.pone.0186442. PMID: 29040295. PMID29040295 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/29040295/
RECORD: Rec_0296305 VERIFIED: YES
Provenance & Taxonomy
Synthetic construct [Synthetic]
32630
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
None
Bio-Activity Profile
Antimicrobial Antibacterial Anti-Gram-positive Antifungal
Candida albicans
512 μg/mL
MIC
PaperHydrophobic residues are critical for the helix-forming, hemolytic and bactericidal activities of amphipathic antimicrobial peptide TP4. PLoS One. 2017 Oct 17;12(10):e0186442. doi: 10.1371/journal.pone.0186442. PMID: 29040295. PMID29040295 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/29040295/
RECORD: Rec_0321255 VERIFIED: YES
Provenance & Taxonomy
Synthetic construct [Synthetic]
32630
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
None
Bio-Activity Profile
Antimicrobial Antibacterial Anti-Gram-positive Antifungal
Methicillin-resistant Staphylococcus aureus
128 μg/mL
MIC
PaperHydrophobic residues are critical for the helix-forming, hemolytic and bactericidal activities of amphipathic antimicrobial peptide TP4. PLoS One. 2017 Oct 17;12(10):e0186442. doi: 10.1371/journal.pone.0186442. PMID: 29040295. PMID29040295 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/29040295/
RECORD: Rec_0352691 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Defensin
32630.0
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Antibacterial Antifungal Anti-Gram-positive Anti-Gram-negative
Candida albicans
512 μg/mL
MIC
PMID29040295 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/29040295/
RECORD: Rec_0361822 VERIFIED: YES
Provenance & Taxonomy
synthetic construct [Synthetic]
Defensin
32630.0
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Antibacterial Antifungal Anti-Gram-positive Anti-Gram-negative
MRSA
128 μg/mL
MIC
PMID29040295 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/29040295/
FIRST PREV 1 2 3 NEXT LAST
Showing 5 records on this page · Page 2 of 3