The Ph.D.-C7C Phage Display Peptide Library is based on a combinatorial library of random peptides fused to a minor coat protein (pIII) of M13 phage (1–6). Unlike other Phage Display Libraries from NEB, the randomized sequence is flanked by a pair of cysteine residues. Under nonreducing conditions the cysteines will spontaneously form a disulfide cross-link, resulting in phage display of cyclized peptides. Disulfide-constrained peptide libraries (7) have proven useful in identification of structural epitopes (8,9), mirror-image ligands for D-amino acid targets (10) and leads for peptide-based therapeutics (11). The disulfide-constrained heptapeptides are expressed at the N-terminus of plll, with the first cysteine preceded by an alanine residue and the second cysteine followed by a short spacer (Gly-Gly-Gly-Ser) and then the wild-type plll sequence. The library consist of 109 electroporated sequences amplified once to yield approximately 100 copies of each sequence in 10 µl of the supplied phage.
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