• Interaction

    AccNo. 47699 Score 0.49
    Name PM_15251031
    Kd 1.0

    Peptide

    AccNo. 47577
    Name YYWLH
    Sequence YYWLHH
    47577_small
    Internalized no
    Is Motif no

    Interactor

    AccNo. 47199
    Name unknown

    Experiment

    AccNo. 47541
    Classification incorrect?
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    Voting_motivation
    CA CVD DM APO ANG MI BD
    0.98 0.59 0.42 0.69 0.62 0.24 0.80 Vote
    plus plus plus plus plus plus plus Yes
    minus minus minus minus minus minus minus No
    Name PM_15251031
    Detection unspecified method, MI:0686
    Source Pubmed Text Id 15251031
    Journal J Pept Res. 2004 Aug;64(2):51-64.
    Title A hexamer peptide ligand that binds selectively to staphylococcal enterotoxin B: isolation from a solid phase combinatorial library.
    Authors Wang G, De J, Schoeniger JS, Roe DC, Carbonell RG
    Text By screening a solid-phase combinatorial peptide library, a short peptide ligand, YYWLHH, has been discovered that binds with high affinity and selectivity to staphylococcal enterotoxin B (SEB), but only weakly to other SEs that share sequence and structural homology with SEB. Using column affinity chromatography with an immobilized YYWLHH stationary phase, it was possible to separate SEB quantitatively from Staphylococcus aureus fermentation broth, a complex mixture of proteins, carbohydrates and other biomolecules. The immobilized peptide was also used to purify native SEB from a mixture containing denatured and hydrolyzed SEB, and showed little cross-reactivity with other SEs. To our knowledge this is the first report of a highly specific short peptide ligand for SEB. Such a ligand is a potential candidate to replace antibodies for detection, removal and purification strategies for SEB.
    Mesh Terms Amino Acid Sequence; Enterotoxins/metabolism; Humans; Ligands; Peptide Library; Peptides/chemistry; Peptides/metabolism; Protein Binding; Staphylococcus aureus/metabolism; Superantigens/metabolism
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