A probe for capture and Fe3+-induced conformational change of lactoferrin selected from phage displayed peptide libraries

Journal of Dairy Science
W NoppeH Deckmyn

Abstract

Linear pentadecamer and cyclic hexamer peptide phage libraries were used to isolate phage clones with binding affinity toward lactoferrins purified from human and bovine milk. Phage clones with high specificity toward lactoferrin were selected with different binding strengths depending on the sequence of the peptide displayed by the phage. Phages coated to a microtiterplate were able to capture lactoferrin from crude milk samples without prior treatment. One of the selected sequences, EGKQRR, failed to bind to lactoferrin. In contrast, a branched tree-peptide bearing 4 EGKQRR sequences did bind to lactoferrin (Kd approximately 29 microM) and was also capable of inhibiting the binding of the phage to lactoferrin (IC(50) approximately 17 microM), indicating that avidity was important. Unexpectedly, the affinity of the phage for lactoferrin was influenced by the amount of bound Fe(3+), with a much lower affinity when lactoferrin was saturated with Fe(3+) as compared with the iron-depleted or partially saturated (natural) lactoferrin. As the phage does not bind to the Fe(3+)-binding site, the difference in binding affinity is due to differences in conformation of lactoferrin induced by Fe(3+). These results demonstrate that avidity...Continue Reading

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Citations

Oct 28, 2005·Journal of Molecular Recognition : JMR·Rebecca L Rich, David G Myszka
Jun 15, 2007·Journal of Animal Science·P LacasseD Petitclerc
Jun 28, 2011·Protein Engineering, Design & Selection : PEDS·Wim NoppeHans Deckmyn

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