General Information

    • DRAMP ID

    • DRAMP30388

    • Peptide Name

    • M1

    • Source

    • Synthetic construct

    • Family

    • Coronaviridae

    • Gene

    • Not found

    • Sequence

    • EANTTLLDLTYEMLSLQQVVKALNESYIDLKEL

    • Sequence Length

    • 33

    • UniProt Entry

    • No entry found

    • Protein Existence

    • Not found

Activity Information

    • Biological Activity

    • Antimicrobial, Antiviral

    • Target Organism

      • [Ref.27795416]MERS-CoV:inhibition of MERS-CoV S-medicated cell-cell fusion in MT-2 cells(IC50=0.9 μM);inhibition of pseudovirus infection in MT-2 cells(IC50=2.3 μM).

    • Hemolytic Activity

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

    • Cytotoxicity

    • No cytotoxicity information found in the reference(s) presented

    • Binding Target

    • membrane

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

    • DRAMP30388 helical wheel diagram

    • PDB ID

    • None

    • Predicted Structure

    • There is no predicted structure for DRAMP30388.

Physicochemical Information

    • Formula

    • C169H277N39O57S

    • Absent Amino Acids

    • CFGHPRW

    • Common Amino Acids

    • L

    • Mass

    • 3799.35

    • PI

    • 4.08

    • Basic Residues

    • 2

    • Acidic Residues

    • 6

    • Hydrophobic Residues

    • 13

    • Net Charge

    • -4

    • Boman Index

    • -3660

    • Hydrophobicity

    • -0.009

    • Aliphatic Index

    • 130

    • Half Life

      • Mammalian:1 hour
      • Yeast:30 min
      • E.coli:>10 hour

    • Extinction Coefficient Cystines

    • 2980

    • Absorbance 280nm

    • 93.13

    • Polar Residues

    • 9

DRAMP30388

DRAMP30388 chydropathy plot

Comments Information

    • Mechanism

    • The peptide inhibits HIV fusion by binding to the hydrophobic grooves on the N-terminal heptad repeat (NHR) trimer and blocking six-helix-bundle (6-HB) formation.

Literature Information

  • ·Literature 1

    • Title

    • Creating an Artificial Tail Anchor as a Novel Strategy To Enhance the Potency of Peptide-Based HIV Fusion Inhibitors.

    • Reference

    • J Virol. 2016 Dec 16;91(1):e01445-16.

    • Author

    • Su S, Zhu Y, Ye S, Qi Q, Xia S, Ma Z, Yu F, Wang Q, Zhang R, Jiang S, Lu L.