MYP_106928
Basic Information
Styelin-D
Antimicrobial
Antimicrobial Antibacterial
Antimicrobial Antibacterial Anti-Gram-negative
Antimicrobial Antibacterial Anti-Gram-positive
Antimicrobial Antifungal
Toxicity / Safety Blood cell toxicity Hemolysis Hemolytic
Venom / Toxin General toxin Toxic
Venom / Toxin General toxin Toxicity
Standard
32 amino acids
C185H277N49O39
Standard
Sequence
GWLRKAAKSVGKFYYKHKYYIKAAWQIGKHAL
Physicochemical Analysis
3811.48 Da
10.24
7.92
7.60
0.2476
-0.57
0.79
-0.02
38.11
73.44
0.2188
16960.00
16960.00
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
1442.64
-5.90
53.0
49.0
126.0
273.0
11.0
32.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0020785 VERIFIED: YES
Provenance & Taxonomy
Styela clava [Animal]
Styelin
Structure & Mods
Single-chain peptide backbone represented as a linear sequence entry [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Antibacterial Antifungal Anti-Gram-positive Anti-Gram-negative
Candida albicans
RECORD: Rec_0031692 VERIFIED: YES
Provenance & Taxonomy
Sea squirt [Animal]
Cecropin
Structure & Mods
linear peptide [Linear]
noncanonical stereochemical modification [Modified]
This peptide is extensively modified: W2 is a 6-bromotryptophan (XXH); R4 is a dihydroxyarginine; K5, K8, K12, and K17 are dihydroxylysines; K19 and K23 are 5-hydroxylysines; and Y15, Y16, Y20 and Y21 are 3,4-dihydroxyphenylalanine (XXK). Such modifications led to heterogeneity as well as enhanced antimicrobial activity (Taylor SW et al. 2000 J Bio Chem 275: 38417-38426)
Bio-Activity Profile
Antimicrobial Toxicity
is more sensitive to these peptides than sheep RBC
40 μg/mL
HC50
RECORD: Rec_0160077 VERIFIED: YES
Provenance & Taxonomy
Sea squirt [Animal]
Cecropin
Structure & Mods
linear peptide [Linear]
noncanonical stereochemical modification [Modified]
This peptide is extensively modified: W2 is a 6-bromotryptophan (XXH); R4 is a dihydroxyarginine; K5, K8, K12, and K17 are dihydroxylysines; K19 and K23 are 5-hydroxylysines; and Y15, Y16, Y20 and Y21 are 3,4-dihydroxyphenylalanine (XXK). Such modifications led to heterogeneity as well as enhanced antimicrobial activity (Taylor SW et al. 2000 J Bio Chem 275: 38417-38426)
Bio-Activity Profile
Antimicrobial Toxicity
human RBC
<10 μg/mL
HC50
RECORD: Rec_0293618 VERIFIED: YES
Provenance & Taxonomy
not reported [other]
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
None
Amidation
W*=6-bromotryptophan,R**=dihydroxyarginine, Y* = 3,4-dihydroxyphenylalanine,K* = 5-hydroxylysine, K**= dihydroxylysine
Bio-Activity Profile
Antimicrobial Toxic Hemolytic
RECORD: Rec_0296857 VERIFIED: NO
Provenance & Taxonomy
Sea squirt [Animal]; Animalia [Animal]
33208; 33208
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial
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