MYP_015981
Basic Information
Temporin-PMb
Anticancer
Antimicrobial
Standard
13 amino acids
C78H112N14O15
Standard
Sequence
FLPFLGKLFSGIF
Physicochemical Analysis
1485.81 Da
8.75
0.76
0.55
0.0584
1.54
0.48
0.67
19.27
120.00
0.3077
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
449.98
1.26
15.0
16.0
45.0
107.0
5.0
12.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0030160 VERIFIED: YES
Provenance & Taxonomy
Lithobates palmipes [Animal]
Temporin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Amidation
isolated from skin secretion via RP-HPLC. Sequence analysis: APD analysis reveals that this sequence is similar (92.31%) to Temporin-PMa F: 31%, L: 23%. GRAVY: 1.538, mol Wt: 1485.832, mol formula: C78H112N14O15, mol ex coeff: 0. It differs from Temporin-PMa only at a single position, F for this peptide and L for AP3610 (PMa). Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial Anticancer
HeLa
32.4 μM
IC50
RECORD: Rec_0106856 VERIFIED: YES
Provenance & Taxonomy
Lithobates palmipes [Animal]
Temporin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Amidation
isolated from skin secretion via RP-HPLC. Sequence analysis: APD analysis reveals that this sequence is similar (92.31%) to Temporin-PMa F: 31%, L: 23%. GRAVY: 1.538, mol Wt: 1485.832, mol formula: C78H112N14O15, mol ex coeff: 0. It differs from Temporin-PMa only at a single position, F for this peptide and L for AP3610 (PMa). Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial Anticancer
but KPC strain MIC>128 uM AMP-resistant? Pseudomonas aeruginosa ATCC 27853
32 μM
MIC
RECORD: Rec_0114419 VERIFIED: YES
Provenance & Taxonomy
Lithobates palmipes [Animal]
Temporin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Amidation
isolated from skin secretion via RP-HPLC. Sequence analysis: APD analysis reveals that this sequence is similar (92.31%) to Temporin-PMa F: 31%, L: 23%. GRAVY: 1.538, mol Wt: 1485.832, mol formula: C78H112N14O15, mol ex coeff: 0. It differs from Temporin-PMa only at a single position, F for this peptide and L for AP3610 (PMa). Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial Anticancer
Klebsiella pneumoniae ATCC 13883
16 μM
MIC
RECORD: Rec_0202420 VERIFIED: YES
Provenance & Taxonomy
Lithobates palmipes [Animal]
Temporin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Amidation
isolated from skin secretion via RP-HPLC. Sequence analysis: APD analysis reveals that this sequence is similar (92.31%) to Temporin-PMa F: 31%, L: 23%. GRAVY: 1.538, mol Wt: 1485.832, mol formula: C78H112N14O15, mol ex coeff: 0. It differs from Temporin-PMa only at a single position, F for this peptide and L for AP3610 (PMa). Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial Anticancer
keratinocytes
25.0 μM
IC50
RECORD: Rec_0263884 VERIFIED: YES
Provenance & Taxonomy
Lithobates palmipes [Animal]
Temporin
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Amidation
isolated from skin secretion via RP-HPLC. Sequence analysis: APD analysis reveals that this sequence is similar (92.31%) to Temporin-PMa F: 31%, L: 23%. GRAVY: 1.538, mol Wt: 1485.832, mol formula: C78H112N14O15, mol ex coeff: 0. It differs from Temporin-PMa only at a single position, F for this peptide and L for AP3610 (PMa). Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial Anticancer
also MRSA MIC>128 uM AMP-resistant? Bacterial resistant strains: A. baunmannii MDR
8 μM
MIC
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