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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_0007509 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.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_0022864 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
Pseudomonas aeruginosa
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_0136240 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
Enterococcus faecalis
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_0177930 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. aerogenes
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_0229405 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
Klebsiella pneumoniae
6.25 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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