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MYP_015381
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Basic Information
2K4L
Antimicrobial
Standard
13 amino acids
C81H147N17O14
Standard
Sequence
IILLLLKKFLKKL
Physicochemical Analysis
1583.14 Da
10.48
3.76
3.55
0.2889
1.46
0.60
0.33
4.45
240.00
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
516.60
3.34
18.0
18.0
59.0
112.0
1.0
12.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0193122 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 2K2L L: 46%, K: 31%, I: 15%. 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_0208693 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 2K2L L: 46%, K: 31%, I: 15%. 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_0265088 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 2K2L L: 46%, K: 31%, I: 15%. 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_0300557 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 2K2L L: 46%, K: 31%, I: 15%. Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial
Klebsiella pneumoniae
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_0349687 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 2K2L L: 46%, K: 31%, I: 15%. 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.
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