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MYP_162580
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Basic Information
4K4L
Antimicrobial
Standard
13 amino acids
C81H149N19O14
Standard
Sequence
KILKLLKKFLKKL
Physicochemical Analysis
1613.17 Da
10.70
5.75
5.54
0.4426
0.22
0.88
-0.09
-15.14
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
568.64
1.51
20.0
20.0
63.0
114.0
1.0
12.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0261454 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 (84.62%) to Temporin-1CEc analog 4K2L K: 46%, L: 38%. Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial
Staphylococcus aureus
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_0265493 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 (84.62%) to Temporin-1CEc analog 4K2L K: 46%, L: 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_0270249 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 (84.62%) to Temporin-1CEc analog 4K2L K: 46%, L: 38%. Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial
E. faecium
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_0369102 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 (84.62%) to Temporin-1CEc analog 4K2L K: 46%, L: 38%. Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial
B. cereus
12.5 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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