General Information

    • DRAMP ID

    • DRAMP29950

    • Peptide Name

    • SA-35

    • Source

    • Synthetic construct

    • Family

    • Paramyxoviridae

    • Gene

    • Not found

    • Sequence

    • MITHGCYTRTRHKHKLKKTL

    • Sequence Length

    • 20

    • UniProt Entry

    • No entry found

    • Protein Existence

    • Not found

Activity Information

    • Biological Activity

    • Antimicrobial, Antiviral

    • Target Organism

      • [Ref.32124885]Respiratory syncytial virus (RSV):SA-35 caused a significant decrease of the RSV infectivity by 33 times at concentrations 1 mg/ml.

    • Hemolytic Activity

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

    • Cytotoxicity

      • [Ref.32124885]MA-104 cells:CC50= 2.1 ± 0.1 mg/ml.

    • 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

    • Not found

    • Structure Description

    • Not found

    • Helical Wheel Diagram

    • DRAMP29950 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

    • There is no predicted structure for DRAMP29950.

Physicochemical Information

    • Formula

    • C107H182N36O26S2

    • Absent Amino Acids

    • ADEFNPQSVW

    • Common Amino Acids

    • KT

    • Mass

    • 2452.97

    • PI

    • 10.58

    • Basic Residues

    • 9

    • Acidic Residues

    • 0

    • Hydrophobic Residues

    • 3

    • Net Charge

    • +9

    • Boman Index

    • -5711

    • Hydrophobicity

    • -1.11

    • Aliphatic Index

    • 58.5

    • Half Life

      • Mammalian:30 hour
      • Yeast:>20 hour
      • E.coli:>10 hour

    • Extinction Coefficient Cystines

    • 1490

    • Absorbance 280nm

    • 78.42

    • Polar Residues

    • 7

DRAMP29950

DRAMP29950 chydropathy plot

Comments Information

    • Mechanism

    • It is likely that these peptides exert anti-RSV activity through a combination of two mechanisms

Literature Information

  • ·Literature 1

    • Title

    • Linear and dendrimeric antiviral peptides: design, chemical synthesis and activity against human respiratory syncytial virus.

    • Reference

    • J Mater Chem B. 2020 Apr 1;8(13):2607-2617

    • Author

    • Kozhikhova KV, Shilovskiy IP, Shatilov AA, Timofeeva AV, Turetskiy EA, Vishniakova LI, Nikolskii AA, Barvinskaya ED, Karthikeyan S, Smirnov VV, Kudlay DA, Andreev SM, Khaitov MR