Peptide Database

Peptide NameHYL-3 (Derived from HYL)

Function Ontology

Antimicrobial

Antimicrobial ▸ Antibacterial

Antimicrobial ▸ Antibacterial ▸ Anti-Gram-negative

Antimicrobial ▸ Antibacterial ▸ Anti-Gram-positive

Antimicrobial ▸ Antifungal

Toxicity / Safety ▸ Blood cell toxicity ▸ Hemolysis ▸ Hemolytic

Standard StatusStandard

Sequence Length16 amino acids

Chemical FormulaC78H142N22O19S2

DescriptionStandard

        GIMSSLMKKLAAHIKK
    

Molecular Weight1756.23 Da

Isoelectric Point (pI)10.48

Net Charge (pH 7.0)3.84

Net Charge (pH 7.4) 3.58

Charge Density (pH 7.0) 0.2402

GRAVY Index0.20

Hydrophobic Moment 0.60

Boman Index0.07

Instability Index55.11

Aliphatic Index 110.00

Aromaticity 0.0000

Extinction Coeff. Reduced 0.00

Extinction Coeff. Oxidized 0.00

The radar chart summarizes major physicochemical dimensions for quick comparison, while exact numerical values remain listed on the left.

Amino Acid Composition

TPSA 673.04

LogP -4.50

H-bond Donors 24.0

H-bond Acceptors 26.0

Rotatable Bonds 65.0

Heavy Atoms 121.0

Ring Count 1.0

Amide Bonds 15.0

3D PDB MODEL

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2D CHEMICAL STRUCTURE

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RECORD: Rec_0010959 VERIFIED: YES

Provenance & Taxonomy

OrganismSynthetic construct [Synthetic]

Tax ID32630

Structure & Mods

Configlinear peptide [Linear]

Chiralitycanonical L-amino-acid peptide [L]

N-TermNone

C-TermAmidation

Bio-Activity Profile

Function

Antimicrobial Antibacterial Anti-Gram-positive Anti-Gram-negative Antifungal

TargetPseudomonas aeruginosa 5482

Activity23 μM

MethodMIC

PaperAntimicrobial Peptide from the Wild Bee Hylaeus signatus Venom and Its Analogues: Structure-Activity Study and Synergistic Effect with Antibiotics. J Nat Prod. 2016 Apr 22;79(4):1073-83. doi: 10.1021/acs.jnatprod.5b01129. PMID: 26998557. PMID26998557 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/26998557/

RECORD: Rec_0067097 VERIFIED: YES

Provenance & Taxonomy

OrganismHylaeus signatus [Animal]

Structure & Mods

Configlinear peptide [Linear]

Chiralitycanonical L-amino-acid peptide [L]

C-TermAmidation

Bio-Activity Profile

Function

Antimicrobial Antibacterial Antifungal Anti-Gram-positive Anti-Gram-negative

TargetEscherichia coli

Activity20 μM

MethodMIC

RECORD: Rec_0077879 VERIFIED: YES

Provenance & Taxonomy

OrganismSynthetic construct [Synthetic]

Tax ID32630

Structure & Mods

Configlinear peptide [Linear]

Chiralitycanonical L-amino-acid peptide [L]

N-TermNone

C-TermAmidation

Bio-Activity Profile

Function

Antimicrobial Antibacterial Anti-Gram-positive Anti-Gram-negative Antifungal

TargetStaphylococcus aureus 6271

Activity85 μM

MethodMIC

PaperAntimicrobial Peptide from the Wild Bee Hylaeus signatus Venom and Its Analogues: Structure-Activity Study and Synergistic Effect with Antibiotics. J Nat Prod. 2016 Apr 22;79(4):1073-83. doi: 10.1021/acs.jnatprod.5b01129. PMID: 26998557. PMID26998557 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/26998557/

RECORD: Rec_0091066 VERIFIED: YES

Provenance & Taxonomy

OrganismSynthetic construct [Synthetic]

Tax ID32630

Structure & Mods

Configlinear peptide [Linear]

Chiralitycanonical L-amino-acid peptide [L]

N-TermNone

C-TermAmidation

Bio-Activity Profile

Function

Antimicrobial Antibacterial Anti-Gram-positive Anti-Gram-negative Antifungal Hemolytic

Targethuman red blood cells

Activity400 μM

MethodLC50

PaperAntimicrobial Peptide from the Wild Bee Hylaeus signatus Venom and Its Analogues: Structure-Activity Study and Synergistic Effect with Antibiotics. J Nat Prod. 2016 Apr 22;79(4):1073-83. doi: 10.1021/acs.jnatprod.5b01129. PMID: 26998557. PMID26998557 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/26998557/

RECORD: Rec_0218965 VERIFIED: YES

Provenance & Taxonomy

OrganismHylaeus signatus [Animal]

Structure & Mods

Configlinear peptide [Linear]

Chiralitycanonical L-amino-acid peptide [L]

C-TermAmidation

Bio-Activity Profile

Function

Antimicrobial Antibacterial Antifungal Anti-Gram-positive Anti-Gram-negative

TargetStaphylococcus aureus 6271

Activity85 μM

MethodMIC

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