• • DRAMP ID

  • DRAMP29049

• • Peptide Name

  • Ano-1β (variant of Anoplin)

• • Source

  • Synthetic construct (Ano-1β is a variant of Anoplin, which is a linear cationic α-helical AMPs isolated from the venom sac of anoplius samariensis(solitary spider wasps))

• • Family

  • Not found

• • Gene

  • N/A

• • Sequence

  • ALLKRIKTLL

• • Sequence Length

  • 10

• • UniProt Entry

  • No entry found

• • Protein Existence

  • Synthetic form

• • Biological Activity

  • Antimicrobial, Antibacterial, Anti-Gram+, Anti-Gram-

• • Target Organism

  • • [Ref.32654770] Gram-negative multidrug-resistant bacteria: P. aeruginosa 119 (MIC = 8 μM or 8.93 μg/mL), P. aeruginosa 124 (MIC = 8 μM or 8.93 μg/mL), P. aeruginosa 86 (MIC = 4 μM or 4.47 μg/mL);
    • Gram-negative bacteria: P. aeruginosa ATCC 27853 (MIC = 8 μM or 8.93 μg/mL), P. aeruginosa ATCC 9027 (MIC = 8 μM or 8.93 μg/mL), E. coli ATCC 25922 (MIC = 32 μM or 35.72 μg/mL), K. pneumonia ATCC 700603 (MIC = 32 μM or 35.72 μg/mL), A. baumannii ATCC 19606 (MIC = 64 μM or 71.44 μg/mL);
    • Gram-positive bacteria: S. aureus ATCC 25923 (MIC = 128 μM or 142.88 μg/mL), S. epidermidis ATCC 12228 (MIC = 8 μM or 8.93 μg/mL)

• • Hemolytic Activity

  • • [Ref.32654770]Ano-1β induced inappreciable hemolytic activity with less than 5 % hemolysis at all the tested concentrations and HC > 256 μM. Note: Minimum hemolysis concentration (HC, μM) was defined as the minimal peptide concentration induced 10 % hemolysis.

• • Cytotoxicity

  • • [Ref.32654770]After 1 h of incubation, Ano-1β, similar to their parent peptide anoplin, maintained more than 80 % cell viability of the two cells at all tested concentrations. After incubating for 24 h, Ano-1β still maintained more than 80 % cell viability of HEK 293 T cells at all tested concentrations but displayed cytotoxicity against Hela cells at the highest concentration (256 μM). The cell viability of Hela after 24 h of incubation is around 80%.

• • Binding Target

  • Membrane

• • Linear/Cyclic

  • Linear

• • N-terminal Modification

  • Free

• • C-terminal Modification

  • Amidation

• • Nonterminal Modifications and Unusual Amino Acids

  • [Ref.32654770] The residue A at position 1 indicates the β-Ala

• • Stereochemistry

  • L

• • Structure

  • 75.3% α-helical content in 30 mM SDS

• • Structure Description

  • As shown in Fig. 1, the new peptides displayed mostly unordered conformations in the aqueous environment as demonstrated by a negative peak at approximately 195 nm. However, in 30 mM SDS, the new peptides folded typical α-helical conformations, as evidenced by a characteristic positive peak at approximately 195 nm and double negative peaks at approximately 208 nm and 222 nm. 

• • Helical Wheel Diagram

  • 

• • PDB ID

  • None

• Predicted Structure

• There is no predicted structure for DRAMP29049.

DRAMP29049

• • Comment

  • the incorporation of β-Ala had significant influence on the antimicrobial activity of peptides mainly due to the changes of hydrophobicity and net positive charge. Ano-1β exhibited good antimicrobial potency, which was stable under physiological conditions and displayed preferable in vivo antimicrobial activity with less acute toxicity. In particular, Ano-1β showed low tendency to develop bacterial resistance in contrast to conventional antibiotics rifampicin and gentamicin, and they exhibited better anti-biofilm activity and synergistic or additive effects in combination with conventional antibiotics. Ano-1β might stands as a promising antimicrobial candidate to overcome increasing bacterial resistance, and the incorporation of β-Ala was a reasonable strategy for the development of promising antimicrobial agents.

• ·Literature 1

• • Title

  • Synthesis and anti-pseudomonal activity of new ß-Ala modified analogues of the antimicrobial peptide anoplin

• • Pubmed ID

  • 32654770

• • Reference

  • Int J Med Microbiol. 2020 Jul;310(5):151433. doi: 10.1016/j.ijmm.2020.151433. Epub 2020 May 27.

• • Author

  • Zhong C, Zhu Y, Zhu N, Liu T, Gou S, Zhang F, Yao J, Xie J, Ni J