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MYP_064078
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Basic Information
2K2L
Antimicrobial
Standard
13 amino acids
C79H139N17O14
Standard
Sequence
IIPLPLKKFLKKL
Physicochemical Analysis
1551.05 Da
10.48
3.76
3.55
0.2889
0.63
0.57
0.19
2.24
180.00
0.0769
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
499.02
2.26
16.0
18.0
53.0
110.0
3.0
12.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0060376 VERIFIED: YES
Provenance & Taxonomy
synthetic construct based on Rana chensinensis [Synthetic]
Temporin
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
Amidation
APD analysis reveals that this sequence is similar (69.23%) to Temporin-1CEc K=L: 31%, P: 15%. Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial
Pseudomonas aeruginosa
6.25 μM
MIC
PaperMembrane mechanism of temporin-1CEc, an antimicrobial peptide isolated from the skin secretions of Rana chensinensis, and its systemic analogs.
RECORD: Rec_0085134 VERIFIED: YES
Provenance & Taxonomy
synthetic construct based on Rana chensinensis [Synthetic]
Temporin
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
Amidation
APD analysis reveals that this sequence is similar (69.23%) to Temporin-1CEc K=L: 31%, P: 15%. Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial
E. aerogenes
3.13 μM
MIC
PaperMembrane mechanism of temporin-1CEc, an antimicrobial peptide isolated from the skin secretions of Rana chensinensis, and its systemic analogs.
RECORD: Rec_0135950 VERIFIED: YES
Provenance & Taxonomy
synthetic construct based on Rana chensinensis [Synthetic]
Temporin
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
Amidation
APD analysis reveals that this sequence is similar (69.23%) to Temporin-1CEc K=L: 31%, P: 15%. Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial
Escherichia coli
25 μM
MIC
PaperMembrane mechanism of temporin-1CEc, an antimicrobial peptide isolated from the skin secretions of Rana chensinensis, and its systemic analogs.
RECORD: Rec_0139886 VERIFIED: YES
Provenance & Taxonomy
synthetic construct based on Rana chensinensis [Synthetic]
Temporin
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
Amidation
APD analysis reveals that this sequence is similar (69.23%) to Temporin-1CEc K=L: 31%, P: 15%. Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial
E.cloacae
>100 μM
MIC
PaperMembrane mechanism of temporin-1CEc, an antimicrobial peptide isolated from the skin secretions of Rana chensinensis, and its systemic analogs.
RECORD: Rec_0203899 VERIFIED: YES
Provenance & Taxonomy
synthetic construct based on Rana chensinensis [Synthetic]
Temporin
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
Amidation
APD analysis reveals that this sequence is similar (69.23%) to Temporin-1CEc K=L: 31%, P: 15%. Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial
Staphylococcus aureus
25 μM
MIC
PaperMembrane mechanism of temporin-1CEc, an antimicrobial peptide isolated from the skin secretions of Rana chensinensis, and its systemic analogs.
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