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MYP_053043
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Basic Information
Histatin5
Antimicrobial
Antimicrobial ▸ Antibacterial
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-negative
Antimicrobial ▸ Antibacterial ▸ Anti-Gram-positive
Antimicrobial ▸ Anti-biofilm ▸ Biofilm inhibition
Antimicrobial ▸ Antifungal
Antiparasitic ▸ Anti-Leishmania ▸ Antileishmanial
Antiparasitic ▸ General antiparasitic ▸ Antiparasitic
Antiviral
Other / Curated residual function label ▸ Generic enzyme inhibition annotation
Toxicity / Safety ▸ Blood cell toxicity ▸ Hemolysis ▸ Hemolytic
Venom / Toxin ▸ General toxin ▸ Toxic
Standard
24 amino acids
C133H195N51O33
Standard
Sequence
DSHAKRHHGYKRKFHEKHHSHRGY
Physicochemical Analysis
3036.29 Da
10.28
5.37
4.80
0.2237
-2.45
0.38
-0.63
37.87
4.17
0.1250
2980.00
2980.00
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
1378.68
-14.64
51.0
45.0
102.0
217.0
10.0
23.0
Structural Visualization
3D PDB MODEL
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2D CHEMICAL STRUCTURE
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Experimental Records
RECORD: Rec_0028006 VERIFIED: YES
Provenance & Taxonomy
Homo sapiens [Animal]
Histatin
9606
Structure & Mods
linear peptide [Linear]
mixed L/D amino-acid peptide [Mixed]
allo-residue reported
Bio-Activity Profile
Antimicrobial Antifungal Antiviral
S. mutans cariogenic bacteria
92 μM
ED50
PaperHistatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans.
RECORD: Rec_0033145 VERIFIED: YES
Provenance & Taxonomy
not reported [other]
Structure & Mods
linear peptide; DSSP H 12.5%, E 0.0%, T 37.5%, C 50.0% [Linear]
canonical L-amino-acid peptide [L]
None
None
Bio-Activity Profile
Antibacterial Antiviral Antiparasitic Antimicrobial Antifungal Anti-Gram-positive Antileishmanial Anti-Gram-negative Enzyme Inhibitor
PaperYADAMP: yet another database of antimicrobial peptides PMID22325123 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22325123/
RECORD: Rec_0038152 VERIFIED: NO
Provenance & Taxonomy
Homo sapiens [Animal]
Histatin
9606
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Antibacterial Antifungal
RECORD: Rec_0041347 VERIFIED: YES
Provenance & Taxonomy
Homo sapiens [Animal]
Histatin
9606
Structure & Mods
linear peptide [Linear]
mixed L/D amino-acid peptide [Mixed]
allo-residue reported
Bio-Activity Profile
Antimicrobial Antifungal Antiviral
Derivatives were subjected to clinical trials. Surface immobilized peptide: Dhvar5 has been covalently immobilized 2015 to chitosan film at 2 ng/cm2 and can decrease MRSA
0.5 μg/mL
MIC
PaperHistatins, a novel family of histidine-rich proteins in human parotid secretion. Isolation, characterization, primary structure, and fungistatic effects on Candida albicans.
RECORD: Rec_0078643 VERIFIED: YES
Provenance & Taxonomy
Homo sapiens [Animal]
Histatin
9606
Structure & Mods
linear peptide [Linear]
canonical L-amino-acid peptide [L]
Bio-Activity Profile
Antimicrobial Antibacterial Antifungal Anti-Gram-positive
Candida albicans ATCC 90028
64.45 μg/mL
MIC
PMID31417503 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/31417503/
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