کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
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5371449 | 1503951 | 2011 | 6 صفحه PDF | دانلود رایگان |
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.
Research highlights⺠Salt bridge mutations didn't greatly affect the secondary structure formation of PrP. ⺠Salt bridges of PrP made the interaction with the T2 antibody stronger. ⺠Salt bridges are necessary for structural changes in PrP when interacting with T2.
Journal: Biophysical Chemistry - Volume 156, Issues 2â3, July 2011, Pages 140-145