Affinity panning of a library of peptides displayed on bacteriophages reveals the binding specificity of BiP

Sylvie Blond-Elguindi, Steven E. Cwirla, William J. Dower, Robert J. Lipshutz, Stephen R. Sprang, Joseph F. Sambrook, Mary Jane H. Gething

Research output: Contribution to journalArticlepeer-review

Abstract

We have used affinity panning of libraries of bacteriophages that display random octapeptide or dodecapeptide sequences at the N-terminus of the adsorption protein (plll) to characterize peptides that bind to the endoplasmic reticulum chaperone BiP and to develop a scoring system that predicts potential BiP-binding sequences in naturally occurring polypeptides. BiP preferentially binds peptides containing a subset of aromatic and hydrophobic amino acids in alternating positions, suggesting that peptides bind in an extended conformation, with the side chains of alternating residues pointing into a cleft on the BiP molecule. Synthetic peptides with sequences corresponding to those displayed by BiP-binding bacteriophages bind to BiP and stimulate its ATPase activity, with a half-maximal concentration in the range 10-60 μM.

Original languageEnglish
Pages (from-to)717-728
Number of pages12
JournalCell
Volume75
Issue number4
DOIs
StatePublished - Nov 19 1993

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