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Sökning: onr:"swepub:oai:lup.lub.lu.se:c4b5a003-c536-4c92-958c-4b85450f900d" > A probe for capture...

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

Noppe, W (författare)
Vanhoorelbeke, K (författare)
Galaev, Igor, (författare)
Lunds universitet, Lund University, Naturvetenskapliga fakulteten, Faculty of Science, Kemiska institutionen, Department of Chemistry, Centrum för tillämpade biovetenskaper, Center for Applied Life Sciences, Bioteknik, Biotechnology
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Mattiasson, Bo, (författare)
Lunds universitet, Lund University, Naturvetenskapliga fakulteten, Faculty of Science, Kemiska institutionen, Department of Chemistry, Centrum för tillämpade biovetenskaper, Center for Applied Life Sciences, Bioteknik, Biotechnology
Deckmyn, H (författare)
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Lunds universitet Bioteknik. (creator_code:org_t)
2004
Engelska.
Ingår i: Journal of Dairy Science. - American Dairy Science Association. - 1525-3198. ; 87:10, s. 3247-3255
  • Tidskriftsartikel (refereegranskat)
Abstract Ämnesord
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  • 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 (Kdsimilar to29 muM) and was also capable of inhibiting the binding of the phage to lactoferrin (IC(50)similar to17 muM), indicating that avidity was important. Unexpectedly, the affinity of the phage for lactoferrin was influenced by the amount of bound Fe3+, with a much lower affinity when lactoferrin was saturated with Fe3+ as compared with the iron-depleted or partially saturated (natural) lactoferrin. As the phage does not bind to the Fe3+-binding site, the difference in binding affinity is due to differences in conformation of lactoferrin induced by Fe3+. These results demonstrate that avidity or multipoint attachment and Fe3+-induced conformational changes play an important role in the binding of the selected phage to lactoferrin. Thus, we could demonstrate that, by the use of selected phage clones, we are able not only to detect lactoferrin, but also to capture lactoferrin from crude milk samples. Furthermore, the extent of phage binding provides additional information about the iron content and the concomitant conformation of lactoferrin.

Ämnesord

TEKNIK OCH TEKNOLOGIER  -- Industriell bioteknik (hsv//swe)
ENGINEERING AND TECHNOLOGY  -- Industrial Biotechnology (hsv//eng)

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Av författaren/redakt...
Noppe, W
Vanhoorelbeke, K
Galaev, Igor
Mattiasson, Bo
Deckmyn, H
Om ämnet
TEKNIK OCH TEKNOLOGIER
TEKNIK OCH TEKNO ...
och Industriell biot ...
Artiklar i publikationen
Journal of Dairy ...
Av lärosätet
Lunds universitet

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