Filamentous phage can be cross-linked to make a hydrophilic aggregate
that is pelleted by low-speed centrifugation. The aggregate is stable
at near-neutral pHs, and withstands exposure to the acid buffers (pH d
own to 2.2) that are often used as eluents in immunoaffinity purificat
ion. If a peptide epitope is genetically fused to a coat protein on th
e virion surface! the aggregate serves as an effective affinity matrix
for absorbing and affinity-purifying antibodies that bind the peptide
. When the peptide epitope is first obtained in this form by selection
from large phage display libraries, this ability to fashion an affini
ty matrix directly from the selected phage represents a significant st
reamlining of research and development. (C) 1998 Elsevier Science B.V.
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