General Information

    • DRAMP ID

    • DRAMP29053

    • Peptide Name

    • RcAlb-PepI (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

    • AKLIPTIAL

    • Sequence Length

    • 9

    • 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 = 102 μM, MIC90 > 250 μM, MBC > 250 μM), K. pneumoniae(MIC50 = 121 μM, MIC90 > 250 μM, MBC > 250 μM)
      • Gram-positive bacteria: S. aureus (MIC50 = 123 μM, MIC90 > 250 μM, MBC > 250 μM)
      • Yeast: C. albicans (MIC50 = 62 μM, MIC90 > 250 μM, MFC > 250 μM), C. parapsilosis (MIC50 = 14 μM, MIC90 = 32 μM, MFC = 103 μM), C. tropicalis (MIC50 = 21 μM, MIC90 = 38 μM, MFC = 127 μM)

    • Hemolytic Activity

      • No hemolysis information or data found in the reference(s) presented in this entry

    • Cytotoxicity

      • Not found

    • Binding Target

    • Not found

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

    • DRAMP29053 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

    • There is no predicted structure for DRAMP29053.

Physicochemical Information

    • Formula

    • C45H82N10O11

    • Absent Amino Acids

    • CDEFGHMNQRSVWY

    • Common Amino Acids

    • AIL

    • Mass

    • 939.21

    • PI

    • 8.8

    • Basic Residues

    • 1

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 6

    • Net Charge

    • +1

    • Boman Index

    • 1518

    • Hydrophobicity

    • 1.556

    • Aliphatic Index

    • 195.56

    • Half Life

      • Mammalian:4.4 hour
      • Yeast:>20 hour
      • E.coli:>10 hour

    • Extinction Coefficient Cystines

    • 0

    • Absorbance 280nm

    • 0

    • Polar Residues

    • 1

DRAMP29053

Comments Information

    • Comment

    • RcAlb-PepI 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