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Critical amino acid residues for the specific binding of the Ti-recognizing recombinant ferritin with oxide surfaces of titanium and silicon.
- Source :
-
Langmuir : the ACS journal of surfaces and colloids [Langmuir] 2009 Sep 15; Vol. 25 (18), pp. 10901-6. - Publication Year :
- 2009
-
Abstract
- The interactions of ferritins fused with a Ti-recognizing peptide (RKLPDA) and their mutants with titanium oxide substrates were explored with an atomic force microscope (AFM). The amino acid sequence of the peptide was systematically modified to elucidate the role of each amino acid residue in the specific interaction. Force measurements revealed a clear correlation among the sequences in the N-terminal domain of ferritin, surface potentials, and long-range electrostatic interactions. Measurements of adhesion forces clearly revealed that hydrogen bonds take part in the specific binding as well as the electrostatic interaction between charged residues and surface charges of Ti oxides. Moreover, our results indicated that not only the charged and polar residues but also a neutral residue (proline) govern the strength of the specific binding, with the order of the residues also being significant. These results demonstrate that the local structure of the peptide governs the special arrangement of charged residues and strongly affects the strength of the bindings.
- Subjects :
- Adhesiveness
Amino Acids genetics
Animals
Ferritins genetics
Hydrogen Bonding
Microscopy, Atomic Force
Models, Molecular
Mutant Proteins chemistry
Mutant Proteins genetics
Mutant Proteins metabolism
Mutation genetics
Protein Binding
Protein Structure, Tertiary
Recombinant Fusion Proteins chemistry
Recombinant Fusion Proteins genetics
Static Electricity
Substrate Specificity
Titanium chemistry
Amino Acids metabolism
Ferritins chemistry
Ferritins metabolism
Oxides metabolism
Recombinant Fusion Proteins metabolism
Silicon metabolism
Titanium metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 0743-7463
- Volume :
- 25
- Issue :
- 18
- Database :
- MEDLINE
- Journal :
- Langmuir : the ACS journal of surfaces and colloids
- Publication Type :
- Academic Journal
- Accession number :
- 19735142
- Full Text :
- https://doi.org/10.1021/la901242q