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MYP_105969
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Basic Information
2K
Antimicrobial
Standard
13 amino acids
C74H129N17O15
Standard
Sequence
IIPLPLKKFAKKT
Physicochemical Analysis
1496.92 Da
10.48
3.76
3.55
0.2889
0.13
0.55
0.07
15.30
127.69
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
519.25
-0.43
17.0
19.0
50.0
106.0
3.0
12.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0175016 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 K: 31%, L=P: 15%. Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial
E. faecium
50 μM
MIC
PaperMembrane mechanism of temporin-1CEc, an antimicrobial peptide isolated from the skin secretions of Rana chensinensis, and its systemic analogs.
RECORD: Rec_0217680 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 K: 31%, L=P: 15%. Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial
Staphylococcus aureus
>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_0326000 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 K: 31%, L=P: 15%. Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial
Escherichia coli
>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_0337429 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 K: 31%, L=P: 15%. Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial
Enterococcus faecalis
50 μM
MIC
PaperMembrane mechanism of temporin-1CEc, an antimicrobial peptide isolated from the skin secretions of Rana chensinensis, and its systemic analogs.
RECORD: Rec_0408695 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 K: 31%, L=P: 15%. Chemical modification: C-terminal amidation
Bio-Activity Profile
Antimicrobial
Klebsiella pneumoniae
>100 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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