Y. Katakura et al., THE IMPORTANCE OF IONIC-STRENGTH AS A PARAMETER IN SCREENING PEPTIDE LIGANDS FROM A PHAGE DISPLAY LIBRARY, Journal of fermentation and bioengineering, 85(4), 1998, pp. 447-450
Peptide ligands which bound to a model monomeric protein, bovine pancr
eatic ribonuclease A, could be isolated from a constrained random hexa
peptide phage library. Selection was successful in a low ionic strengt
h buffer (10 mM sodium phosphate, pH 6.0), whereas it failed in TBS (5
0 mM Tris-Cl, 150 mM NaCl, pH 7.5). Two of the displayed amino acid se
quences from among the clones isolated were AEGACEQLDYNC and AEGACLWHD
QLC. Electrostatic interaction appeared to play an important role in t
he binding because these phages could not bind to RNase A at a high io
nic strength. The results suggest that selection in low ionic strength
buffers could make possible the isolation of peptide ligands against
proteins of interest which do not originally interact with another pep
tide or protein.