General Information

    • DRAMP ID

    • DRAMP29054

    • Peptide Name

    • RcAlb-PepII (designed in silico using as template the amino acid sequence of Rc-2S-Alb)

    • Source

    • Synthetic construct (Rc-2S-Alb comes from Ricinus communis (Castor bean))

    • Family

    • Not found

    • Gene

    • N/A

    • Sequence

    • SLRGCC

    • Sequence Length

    • 6

    • UniProt Entry

    • No entry found

    • Protein Existence

    • Synthetic form

Activity Information

    • Biological Activity

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

    • Target Organism

      • [Ref.31678367] Gram-negative bacteria: E. coli (MIC50 = 31 μM, MIC90 = 29 μM, MBC > 250 μM), K. pneumoniae(MIC50 = 11 μM, MIC90 = 21 μM, MBC = 42 μM)
      • Gram-positive bacteria: S. aureus (MIC50 = 79 μM, MIC90 > 250 μM, MBC > 250 μM)
      • Yeast: C. albicans (MIC50 = 129 μM, MIC90 > 250 μM, MFC > 250 μM), C. parapsilosis (MIC50 = 9 μM, MIC90 = 17 μM, MFC = 25 μM), C. tropicalis (MIC50 = 29 μM, MIC90 = 28 μM, MFC = 67 μM)

    • Hemolytic Activity

      • [Ref.31678367] RcAlb-PepII was not harmful to human erythrocytes, even at a concentration 10 times higher than the MBC and MFC for K. pneumoniae and C. parapsilosis, respectively.

    • Cytotoxicity

      • [Ref.31678367] At 420 μM concentration (10 and 16.8 times higher than the MBC and MFC for K. pneumoniae and C. parapsilosis, respectively) RcAlb-PepII reduced only in 21.5% the Vero cell viability

    • Binding Target

    • Intracellular targets

Structure Information

    • Linear/Cyclic

    • Linear

    • N-terminal Modification

    • Free

    • C-terminal Modification

    • Free

    • Nonterminal Modifications and Unusual Amino Acids

    • None

    • Stereochemistry

    • L

    • Structure

    • Partially ordered (non-regular) and α-helical

    • Structure Description

    • RcAlb-PepI and RcAlb-PepII in aqueous solution showed SRCD spectra typical of peptides that present major unordered content of secondary structure. The small (albeit significant) shift of the minimum for the RcAlb-PepII spectrum showed a more partially ordered peptide (although non-canonical) compared with RcAlb-PepI. The SRCD spectra of RcAlb-PepI and RcAlb-PepII in the film were characteristics of partially ordered (non-regular) and α-helix secondary structures.

    • Helical Wheel Diagram

    • DRAMP29054 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

    • There is no predicted structure for DRAMP29054.

Physicochemical Information

    • Formula

    • C23H43N9O8S2

    • Absent Amino Acids

    • ADEFHIKMNPQTVWY

    • Common Amino Acids

    • C

    • Mass

    • 637.77

    • PI

    • 7.8

    • Basic Residues

    • 1

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 1

    • Net Charge

    • +1

    • Boman Index

    • -990

    • Hydrophobicity

    • 0.517

    • Aliphatic Index

    • 65

    • Half Life

      • Mammalian:1.9 hour
      • Yeast:>20 hour
      • E.coli:>10 hour

    • Extinction Coefficient Cystines

    • 125

    • Absorbance 280nm

    • 25

    • Polar Residues

    • 4

DRAMP29054

Comments Information

    • Comment

    • RcAlb-PepII is safe and apparently effective for its intended use and has great potential for the future development of an antimicrobial agent with the ability to kill or inhibit K. pneumoniae and C. parapsilosis cells.

Literature Information

  • ·Literature 1

    • Title

    • RcAlb-PepII, a synthetic small peptide bioinspired in the 2S albumin from the seed cake of Ricinus communis, is a potent antimicrobial agent against Klebsiella pneumoniae and Candida parapsilosis

    • Reference

    • Biochim Biophys Acta Biomembr. 2020 Feb 1;1862(2):183092. doi: 10.1016/j.bbamem.2019.183092. Epub 2019 Oct 31.

    • Author

    • Dias LP, Souza PFN, Oliveira JTA, Vasconcelos IM, Araújo NMS, Tilburg MFV, Guedes MIF, Carneiro RF, Lopes JLS, Sousa DOB