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MYP_160566
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Basic Information
2K4L_W2
Antimicrobial
Standard
13 amino acids
C86H146N18O14
Standard
Sequence
IWLLLLKKFLKKL
Physicochemical Analysis
1656.19 Da
10.48
3.76
3.55
0.2889
1.05
0.59
0.29
-0.87
210.00
0.1538
5500.00
5500.00
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
532.39
4.02
19.0
18.0
59.0
118.0
3.0
12.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0211466 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 (92.31%) to Temporin-1CEc analog 2K4L L: 46%, K: 38%. Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial
S. lactis
1.56 μM
MIC
PaperMembrane mechanism of temporin-1CEc, an antimicrobial peptide isolated from the skin secretions of Rana chensinensis, and its systemic analogs.
RECORD: Rec_0274985 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 (92.31%) to Temporin-1CEc analog 2K4L L: 46%, K: 38%. Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial
Enterococcus faecalis
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_0312142 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 (92.31%) to Temporin-1CEc analog 2K4L L: 46%, K: 38%. Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial
E. faecium
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_0316721 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 (92.31%) to Temporin-1CEc analog 2K4L L: 46%, K: 38%. Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial
E. cloacae
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_0321671 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 (92.31%) to Temporin-1CEc analog 2K4L L: 46%, K: 38%. Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial
B. cereus
0.78 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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