✦ LIBER ✦

Electrosorption of amino acids peptides and proteins in relation to the compatibility of materials and the human body

✍ Scribed by Stoner, Glenn E.

Publisher: John Wiley and Sons
Year: 1969
Tongue: English
Weight: 436 KB
Volume: 3
Category: Article
ISSN: 0021-9304
DOI: 10.1002/jbm.820030409

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✦ Synopsis

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 that electrochemical polymerization of that protein may be the cause of thrombosis at anodes. * All amino acids present in blood proteins were examined except cystine and methionine which are studied in the present work.

** In order for this study to be relevant to peptide or protein adsorption it is necessary that the adsorbability of the amino acid be independent of the dipole moment and only, dependent on the R group of the acid (since the functional group is tied up in the peptide linkage of a protein). This was found to be the case.* * Adsorbed with the two sulphur atoms attached to the metal. **At concentrations above 0.5M. Between .05 and 5.8 X 10-3M, rmal approaches 3.6, i.e., the planar configuration.

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