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Peptide record

TPDB16428

Antibacterial Toxicity modified_plain modified
12 source-reported length (unverified)
Basic Information
TPDB16428
Antibacterial Toxicity
Anti-infective peptides Toxicity and safety peptides
dbAMP Peptipedia
modified_plain
Yes
A modified multi-activity (Antibacterial and Toxicity) peptide record curated from dbAMP and Peptipedia, without an available 3D structural model. Source-reported length: 12 (unverified).
Modified, details unspecified
Sequence
AKRXXGYKRKFX

Source notation is retained verbatim; residue notation and chemical identity have not been independently validated. The displayed length is source-reported and unverified.

Physicochemical Analysis

Sequence-only estimates are not provided for modified or non-standard source notation. Reported molecular properties, when available, are retained below with their source records.

Chemical Descriptors
12 source-reported length (unverified)
Evidence Records 3 records
Evidence 1 Activity

Activity

10% Hemolysis
Toxicity
50 µg/mL
Hemolytic Cytotoxic
10% Hemolysis | 50 | µg/mL | target cell: Human erythrocytes

Target

Human erythrocytes

Source & Reference

NA
DBAASP
Dependence on size and shape of non-nature amino acids in the enhancement of lipopolysaccharide (LPS) neutralizing activities of antimicrobial peptides. | J Colloid Interface Sci | 2019
Evidence 2 Activity

Activity

18% Killing
Toxicity
50 µg/mL
Cytotoxic
18% Killing | 50 | µg/mL | target cell: Human fibroblasts

Target

Human fibroblasts

Source & Reference

NA
DBAASP
Dependence on size and shape of non-nature amino acids in the enhancement of lipopolysaccharide (LPS) neutralizing activities of antimicrobial peptides. | J Colloid Interface Sci | 2019
Evidence 3 Activity

Activity

10% Killing
Toxicity
50 µg/mL
Cytotoxic
10% Killing | 50 | µg/mL | target cell: Human fibroblasts

Target

Human fibroblasts

Source & Reference

NA
DBAASP
Dependence on size and shape of non-nature amino acids in the enhancement of lipopolysaccharide (LPS) neutralizing activities of antimicrobial peptides. | J Colloid Interface Sci | 2019