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MYP_064078
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Basic Information
2K2L
Antimicrobial
Standard
13 amino acids
C79H139N17O14
Standard
Sequence
IIPLPLKKFLKKL
Physicochemical Analysis
1551.05 Da
10.48
3.76
3.55
0.2889
0.63
0.57
0.19
2.24
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
499.02
2.26
16.0
18.0
53.0
110.0
3.0
12.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0205126 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 (69.23%) to Temporin-1CEc K=L: 31%, P: 15%. Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial
Klebsiella pneumoniae
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_0243338 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 (69.23%) to Temporin-1CEc K=L: 31%, P: 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_0275555 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 (69.23%) to Temporin-1CEc K=L: 31%, P: 15%. Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial
S.lactis
>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_0345473 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 (69.23%) to Temporin-1CEc K=L: 31%, P: 15%. Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial
B. cereus
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_0393090 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 (69.23%) to Temporin-1CEc K=L: 31%, P: 15%. 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.
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