Peptide Database

Peptide NameMelectin (MEP; Insects, animals)

Function Ontology

Anticancer

Antimicrobial

Antimicrobial ▸ Antibacterial

Antimicrobial ▸ Antibacterial ▸ Anti-Gram-negative

Antimicrobial ▸ Antibacterial ▸ Anti-Gram-positive

Antimicrobial ▸ Antibiotic activity

Antimicrobial ▸ Antifungal

Antiviral

Antiviral ▸ Anti-HIV ▸ Anti-HIV-1

Antiviral ▸ Antiviral mechanism ▸ Viral entry inhibition

Toxicity / Safety ▸ Blood cell toxicity ▸ Hemolysis ▸ Hemolytic

Toxicity / Safety ▸ Cytolysis / cell lysis ▸ Cytolytic activity

Venom / Toxin ▸ General toxin ▸ Toxic

Standard StatusStandard

Sequence Length18 amino acids

Chemical FormulaC96H166N24O20S2

DescriptionStandard

        GFLSILKKVLPKVMAHMK
    

Molecular Weight2040.62 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) 0.2135

GRAVY Index0.62

Hydrophobic Moment 0.57

Boman Index0.21

Instability Index18.83

Aliphatic Index 124.44

Aromaticity 0.0556

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 702.22

LogP -1.48

H-bond Donors 24.0

H-bond Acceptors 27.0

Rotatable Bonds 71.0

Heavy Atoms 142.0

Ring Count 3.0

Amide Bonds 17.0

3D PDB MODEL

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2D CHEMICAL STRUCTURE

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RECORD: Rec_0286435 VERIFIED: YES

Provenance & Taxonomy

Organismsynthetic construct [Synthetic]

FamilyMEP

Tax ID32630

Structure & Mods

Confighydrocarbon-stapled side-chain cyclic peptide [Cyclic]

Chiralitynoncanonical or residue-modified peptide [Modified]

N-TermNone

C-TermAmidation

Other ModsThe J (position: 14) in sequence indicates norleucine. Ⓧ (position: 5, 9, 13 and 17) are 2-(4'-pentenyl) alanine in the S configuration. Ⓧ (5) and Ⓧ (9), Ⓧ (13) and Ⓧ (17) are cross-linked by hydrocarbon stapling respectively

Bio-Activity Profile

Function

Antimicrobial Antibacterial

TargetPseudomonas aeruginosa

Activity>100 μM

MethodMIC

PaperHubert Chapuis, Jiřina Slaninová, Lucie Bednárová, Lenka Monincová, Miloš Buděšínský, Václav Čeřovský. Effect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera. Amino Acids. 2012 Nov;43(5):2047-58. Epub 2012 Apr 30. PMID22526241 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22526241/

RECORD: Rec_0295424 VERIFIED: YES

Provenance & Taxonomy

Organismsynthetic construct [Synthetic]

FamilyMEP

Tax ID32630

Structure & Mods

Confighydrocarbon-stapled side-chain cyclic peptide [Cyclic]

Chiralitycis-conformation L-amino-acid peptide [Modified]

N-TermNone

C-TermAmidation

Other ModsThe J (position: 14 and 17) in sequence indicates norleucine. Ⓧ (position: 10) is 2-(4'-pentenyl) alanine in the S configuration. Ⓩ (position: 3) is 2-(7'-pctenyl) lalnine in the R configuration. Ⓧ (10) and Ⓩ (3) are cross-linked by hydrocarbon stapling

Bio-Activity Profile

Function

Antimicrobial Antibacterial

TargetStaphylococcus aureus

Activity37 μM

MethodMIC

PaperHubert Chapuis, Jiřina Slaninová, Lucie Bednárová, Lenka Monincová, Miloš Buděšínský, Václav Čeřovský. Effect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera. Amino Acids. 2012 Nov;43(5):2047-58. Epub 2012 Apr 31. PMID22526241 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22526241/

RECORD: Rec_0303347 VERIFIED: YES

Provenance & Taxonomy

Organismsynthetic construct [Synthetic]

FamilyMEP

Tax ID32630

Structure & Mods

Confighydrocarbon-stapled side-chain cyclic peptide [Cyclic]

Chiralitycis-conformation L-amino-acid peptide [Modified]

N-TermNone

C-TermAmidation

Other ModsThe J (position: 14 and 17) in sequence indicates norleucine. Ⓧ (position: 10) is 2-(4'-pentenyl) alanine in the S configuration. Ⓩ (position: 3) is 2-(7'-pctenyl) lalnine in the R configuration. Ⓧ (10) and Ⓩ (3) are cross-linked by hydrocarbon stapling

Bio-Activity Profile

Function

Antimicrobial Antibacterial

TargetBacillus subtilis

Activity1.3 μM

MethodMIC

PaperHubert Chapuis, Jiřina Slaninová, Lucie Bednárová, Lenka Monincová, Miloš Buděšínský, Václav Čeřovský. Effect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera. Amino Acids. 2012 Nov;43(5):2047-58. Epub 2012 Apr 31. PMID22526241 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22526241/

RECORD: Rec_0315669 VERIFIED: YES

Provenance & Taxonomy

OrganismCleptoparasitic bee [Animal]

Structure & Mods

Configlinear peptide [Linear]

Chiralitycanonical L-amino-acid peptide [L]

Bio-Activity Profile

Function

Antimicrobial Antiviral

Targetmethicillin-resistant Staphylococcus aureus (MRSA)

Activity6.8-25 μM

MethodMIC

RECORD: Rec_0326795 VERIFIED: YES

Provenance & Taxonomy

Organismsynthetic construct [Synthetic]

FamilyMEP

Tax ID32630

Structure & Mods

Confighydrocarbon-stapled side-chain cyclic peptide [Cyclic]

Chiralitynoncanonical or residue-modified peptide [Modified]

N-TermNone

C-TermAmidation

Other ModsThe J (position: 14) in sequence indicates norleucine. The Ⓧ (position: 13 and 17) indicates 2-(4'-pentenyl) alanine in the S configuration. Ⓧ (13) and Ⓧ (17) are cross-linked by hydrocarbon stapling

Bio-Activity Profile

Function

Antimicrobial Antibacterial

TargetPseudomonas aeruginosa

Activity77 μM

MethodMIC

PaperHubert Chapuis, Jiřina Slaninová, Lucie Bednárová, Lenka Monincová, Miloš Buděšínský, Václav Čeřovský. Effect of hydrocarbon stapling on the properties of α-helical antimicrobial peptides isolated from the venom of hymenoptera. Amino Acids. 2012 Nov;43(5):2047-58. Epub 2012 Apr 28. PMID22526241 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/22526241/

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