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MYP_145565
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Basic Information
6K-WY2
Antimicrobial
Standard
19 amino acids
C110H192N26O21
Standard
Sequence
KKKKKKFLPFLASLALKIL
Physicochemical Analysis
2214.86 Da
10.78
6.75
6.54
0.3554
0.16
0.48
-0.01
30.95
133.68
0.1053
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
780.70
-0.67
27.0
28.0
81.0
157.0
3.0
18.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0099063 VERIFIED: YES
Provenance & Taxonomy
synthetic construct based on Designed based an [Synthetic]
Temporin
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
Amidation
APD analysis reveals that this sequence is similar (68.42%) to Temporin-WY2 Leu: 26%; K: 37%; F=A: 11%. Chemical modification: C-terminal amidated
Bio-Activity Profile
Antimicrobial
Enterococcus faecalis NCTC 12697
16 μM
MIC
PaperDiscovery and engineering of a novel peptide, Temporin-WY2, with enhanced in vitro and in vivo efficacy against multi-drug resistant bacteria
RECORD: Rec_0120824 VERIFIED: YES
Provenance & Taxonomy
synthetic construct based on Designed based an [Synthetic]
Temporin
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
Amidation
APD analysis reveals that this sequence is similar (68.42%) to Temporin-WY2 Leu: 26%; K: 37%; F=A: 11%. Chemical modification: C-terminal amidated
Bio-Activity Profile
Antimicrobial
Staphylococcus aureus ATCC CRM 6538 or MRSA BAA 1707 or clinical MRSA B038 V1S1 A
4-16 μM
MIC
PaperDiscovery and engineering of a novel peptide, Temporin-WY2, with enhanced in vitro and in vivo efficacy against multi-drug resistant bacteria
RECORD: Rec_0184667 VERIFIED: YES
Provenance & Taxonomy
synthetic construct based on Designed based an [Synthetic]
Temporin
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
Amidation
APD analysis reveals that this sequence is similar (68.42%) to Temporin-WY2 Leu: 26%; K: 37%; F=A: 11%. Chemical modification: C-terminal amidated
Bio-Activity Profile
Antimicrobial
Disrupt preformed biofilms: Escherichia coli
32 μM
MBEC
PaperDiscovery and engineering of a novel peptide, Temporin-WY2, with enhanced in vitro and in vivo efficacy against multi-drug resistant bacteria
RECORD: Rec_0252098 VERIFIED: YES
Provenance & Taxonomy
synthetic construct based on Designed based an [Synthetic]
Temporin
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
Amidation
APD analysis reveals that this sequence is similar (68.42%) to Temporin-WY2 Leu: 26%; K: 37%; F=A: 11%. Chemical modification: C-terminal amidated
Bio-Activity Profile
Antimicrobial
Pseudomonas aeruginosa ATCC 9027 or PA14 or PAO1
4-8 μM
MIC
PaperDiscovery and engineering of a novel peptide, Temporin-WY2, with enhanced in vitro and in vivo efficacy against multi-drug resistant bacteria
RECORD: Rec_0287722 VERIFIED: YES
Provenance & Taxonomy
synthetic construct based on Designed based an [Synthetic]
Temporin
32630
Structure & Mods
synthetic linear peptide [Linear]
canonical L-amino-acid peptide [L]
Amidation
APD analysis reveals that this sequence is similar (68.42%) to Temporin-WY2 Leu: 26%; K: 37%; F=A: 11%. Chemical modification: C-terminal amidated
Bio-Activity Profile
Antimicrobial
Klebsiella pneumoniae ATCC 43816
4 μM
MIC
PaperDiscovery and engineering of a novel peptide, Temporin-WY2, with enhanced in vitro and in vivo efficacy against multi-drug resistant bacteria
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