Peptide Database

Peptide NameUnnamed

Function Ontology

Antimicrobial

Antimicrobial ▸ Antibacterial

Antimicrobial ▸ Antibacterial ▸ Anti-Gram-negative

Antimicrobial ▸ Antibacterial ▸ Anti-Gram-positive

Antimicrobial ▸ Anti-biofilm ▸ Biofilm inhibition

Antiviral

Antiviral ▸ Anti-HIV ▸ Anti-HIV-1

Antiviral ▸ Antiviral mechanism ▸ Viral entry inhibition

Toxicity / Safety ▸ Blood cell toxicity ▸ Hemolysis ▸ Hemolytic

Toxicity / Safety ▸ Cytotoxicity

Venom / Toxin ▸ General toxin ▸ Cytotoxicity

Standard StatusStandard

Sequence Length13 amino acids

Chemical FormulaC82H133N19O14

DescriptionStandard

        FFGKVLKLIRKIF
    

Molecular Weight1609.05 Da

Isoelectric Point (pI)11.26

Net Charge (pH 7.0)3.76

Net Charge (pH 7.4) 3.55

Charge Density (pH 7.0) 0.2890

GRAVY Index0.97

Hydrophobic Moment 0.81

Boman Index0.23

Instability Index-23.42

Aliphatic Index 142.31

Aromaticity 0.2308

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 552.48

LogP 1.07

H-bond Donors 20.0

H-bond Acceptors 18.0

Rotatable Bonds 56.0

Heavy Atoms 115.0

Ring Count 3.0

Amide Bonds 12.0

3D PDB MODEL

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2D CHEMICAL STRUCTURE

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RECORD: Rec_0277985 VERIFIED: YES

Provenance & Taxonomy

Organismsynthetic construct [Synthetic]

FamilyDASamP1

Tax ID32630

Structure & Mods

Configlysine-tethered side-chain stapled peptide [Cyclic]

Chiralitynoncanonical stereochemical modification [Modified]

N-TermNone

C-TermAmidation

Other ModsThe Ⓚ (position: 7 and 11) in sequence indicates Nε-o-Ns-Nα-Fmoc-lysine before stapling. Ⓚ (7) and Ⓚ (11) are cross-linked by a (E)-but-2-enyl spacer employing the N-alkylation reaction

Bio-Activity Profile

Function

Antimicrobial Antibacterial

Targetcephalosporin-resistant Escherichia coli

Activity128 μg/mL

MethodMIC

PaperHu Y, Li H, Qu R, He T, Tang X, Chen W, Li L, Bai H, Li C, Wang W, Fu G, Luo G, Xia X, Zhang J. Lysine Stapling Screening Provides Stable and Low Toxic Cationic Antimicrobial Peptides Combating Multidrug-Resistant Bacteria In Vitro and In Vivo. J Med Chem. 2022 Jan 13;65(1):579-591. PMID34968054 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/34968054/

RECORD: Rec_0325605 VERIFIED: YES

Provenance & Taxonomy

Organismsynthetic construct [Synthetic]

FamilyDASamP1

Tax ID32630

Structure & Mods

Configlysine-tethered side-chain stapled peptide [Cyclic]

Chiralitynoncanonical stereochemical modification [Modified]

N-TermNone

C-TermAmidation

Other ModsThe Ⓚ (position: 7 and 11) in sequence indicates Nε-o-Ns-Nα-Fmoc-lysine before stapling. Ⓚ (7) and Ⓚ (11) are cross-linked by a (E)-but-2-enyl spacer employing the N-alkylation reaction

Bio-Activity Profile

Function

Antimicrobial Antibacterial

TargetStaphylococcus aureus (MRSA)

Activity32 μg/mL

MethodMIC

PaperHu Y, Li H, Qu R, He T, Tang X, Chen W, Li L, Bai H, Li C, Wang W, Fu G, Luo G, Xia X, Zhang J. Lysine Stapling Screening Provides Stable and Low Toxic Cationic Antimicrobial Peptides Combating Multidrug-Resistant Bacteria In Vitro and In Vivo. J Med Chem. 2022 Jan 13;65(1):579-591. PMID34968054 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/34968054/

RECORD: Rec_0340302 VERIFIED: YES

Provenance & Taxonomy

Organismsynthetic construct [Synthetic]

Tax ID32630

Structure & Mods

Configlinear peptide [Linear]

Chiralitycanonical L-amino-acid peptide [L]

Bio-Activity Profile

Function

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

TargetStaphylococcus aureus

Activity3.1 μM

MethodMIC

RECORD: Rec_0351429 VERIFIED: YES

Provenance & Taxonomy

Organismsynthetic construct [Synthetic]

FamilyTemporin

Tax ID32630

Structure & Mods

Configlinear peptide [Linear]

Chiralitycanonical L-amino-acid peptide [L]

N-TermNone

C-TermAmidation

Bio-Activity Profile

Function

Antiviral Anti-HIV-1 Entry inhibition

TargetHIV-1 IIIB | CEM-SS cells

Activity0.63 μM

MethodEC50

Half-LifeMammalian: 1.1 h; Yeast: 3 min; E. coli: 2 min

PaperIdentification of novel human immunodeficiency virus type 1-inhibitory peptides based on the antimicrobial peptide database. | Wang G, Watson KM, Peterkofsky A, Buckheit RW Jr. | Antimicrob Agents Chemother. 2010 Mar;54(3):1343-6. | DOI:10.1128/AAC.01448-09 | PMID:20086159 PMID20086159 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/20086159/

RECORD: Rec_0376288 VERIFIED: YES

Provenance & Taxonomy

Organismsynthetic construct [Synthetic]

FamilyDASamP1

Tax ID32630

Structure & Mods

Configlysine-tethered side-chain stapled peptide [Cyclic]

Chiralitynoncanonical stereochemical modification [Modified]

N-TermNone

C-TermAmidation

Other ModsThe Ⓚ (position: 7 and 11) in sequence indicates Nε-o-Ns-Nα-Fmoc-lysine before stapling. Ⓚ (7) and Ⓚ (11) are cross-linked by a (E)-but-2-enyl spacer employing the N-alkylation reaction

Bio-Activity Profile

Function

Antimicrobial Antibacterial

TargetStaphylococcus aureus BNCC 186335

Activity16 μg/mL

MethodMIC

PaperHu Y, Li H, Qu R, He T, Tang X, Chen W, Li L, Bai H, Li C, Wang W, Fu G, Luo G, Xia X, Zhang J. Lysine Stapling Screening Provides Stable and Low Toxic Cationic Antimicrobial Peptides Combating Multidrug-Resistant Bacteria In Vitro and In Vivo. J Med Chem. 2022 Jan 13;65(1):579-591. PMID34968054 Evidence URLhttps://pubmed.ncbi.nlm.nih.gov/34968054/

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