Title of article :
Salt bridges in prion proteins are necessary for high-affinity binding to the monoclonal antibody T2 Original Research Article
Author/Authors :
Eriko Sasamori، نويسنده , , Mieko Kato، نويسنده , , Kosuke Maki، نويسنده , , Yuichi Tagawa، نويسنده , , Yoshiro Hanyu، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2011
Pages :
6
From page :
140
To page :
145
Abstract :
We studied the role of the 2 salt bridges (Asp143–Arg147 and Asp146–Arg150) in helix 1 of mouse prion protein (PrP) on the formation of the complex between PrP and the monoclonal antibody T2. We introduced 6 charge-changing mutations to the amino acid residues associated with the salt bridges. Analysis of the circular dichroism spectra of the mutant PrPs showed that the salt bridge mutations did not change the secondary structures. We analyzed the kinetics of the association and dissociation of the PrPs with the T2 antibody. The results showed that the association kinetics were not significantly different among the variants except Arg150Lys, while the dissociation rate of the neutralized-charge variants was 2 orders of magnitude higher than that of the wild type. These results indicate that salt bridges make the interaction of PrP with T2 tighter by slowing down dissociation.
Keywords :
Salt bridges , conformation , Mutation , Interaction , antibody , prion protein
Journal title :
Biophysical Chemistry
Serial Year :
2011
Journal title :
Biophysical Chemistry
Record number :
1120464
Link To Document :
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