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MYP_032301
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Basic Information
2K4L_3W
Antimicrobial
Standard
13 amino acids
C96H144N20O14
Standard
Sequence
IWLLLLKKFWKKW
Physicochemical Analysis
1802.30 Da
10.48
3.76
3.55
0.2889
0.32
0.55
0.25
12.19
150.00
0.3077
16500.00
16500.00
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
563.97
5.38
21.0
18.0
59.0
130.0
7.0
12.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0016446 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 (76.92%) to Temporin-1CEc analog 2K4L L: 31%, K: 31%, W: 23%. Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial
Enterococcus faecalis
12.5 μM
MIC
PaperMembrane mechanism of temporin-1CEc, an antimicrobial peptide isolated from the skin secretions of Rana chensinensis, and its systemic analogs.
RECORD: Rec_0063386 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 (76.92%) to Temporin-1CEc analog 2K4L L: 31%, K: 31%, W: 23%. 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_0073228 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 (76.92%) to Temporin-1CEc analog 2K4L L: 31%, K: 31%, W: 23%. Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial
Staphylococcus aureus
0.78 μM
MIC
PaperMembrane mechanism of temporin-1CEc, an antimicrobial peptide isolated from the skin secretions of Rana chensinensis, and its systemic analogs.
RECORD: Rec_0104136 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 (76.92%) to Temporin-1CEc analog 2K4L L: 31%, K: 31%, W: 23%. 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_0248450 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 (76.92%) to Temporin-1CEc analog 2K4L L: 31%, K: 31%, W: 23%. Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial
Escherichia coli
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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