The adsorption behavior of several amino acids, simple peptides and the protein fibrinogin was measured at a charged mercury surface. Evidence was obtained for the significance of r-electron containing amino acid groups in the adsorption of proteins on surfaces. Experiments on fibrinogin indicate th
Electrochemical studies on the adsorption of amino acids in relation to the compatibility of prosthetic materials and the human body
β Scribed by Matthews, Dennis B.
- Publisher
- John Wiley and Sons
- Year
- 1969
- Tongue
- English
- Weight
- 660 KB
- Volume
- 3
- Category
- Article
- ISSN
- 0021-9304
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β¦ Synopsis
The Lippman electrocapillary method was used to survey the adsorption behavior of 25 amino acids at the mercury-solution interface. The amount of surface excess of adsorbed amino acid (I?;), as evidenced by lowering of interfacial tension, was found to increase with the number of double bonds and/or additional nitrogen atoms which provide electron pairs. No influence of dipole moment on adsorption was observed. Adsorption was more extensive at potentials positive to the potential of zero charge, indicating a possible electrontransfer adsorption mechanism, i.e., a sharing ?r-electrons rather than dipole interaction with the metal. These results are consistant with the enhanced adsorption of proteins at anodic potentials since the side groups extending from peptide linkages on a given protein are the R groups of various amino acids.
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