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Electrostatic and hydrophobic effects of oligopeptide insertions on protein adsorption
YKI – Ytkemiska institutet.
1998 (English)In: Journal of Colloid and Interface Science, ISSN 0021-9797, E-ISSN 1095-7103, Vol. 204, 104-111 p.Article in journal (Refereed)
Abstract [en]

The effects of oligopeptide insertions on the adsorption of the protein ZZ, where Z is the IgG binding domain of staphylococcal Protein A, was investigated by in situ ellipsometry. In particular, the interplay between hydrophobic and electrostatic interactions as driving force for adsorption was investigated by studying the effects of oligopeptide insertions of the type Tn(AlaTrpTrpPro), Na ((AlaTrpTrpLysPro)n), and Pn((AlaTrpTrpLysPro)n) on the adsorption at silica, methylated silica , and diaminocyclohexane (DACH) plasma polymer surfaces. For comparison, the adsorption of the inserted peptide stretches was also investigated. It was found that the adsorption of all the peptides increases with the molecular weight at methylated silica. At silica, only the Pn peptides were found to adsorb. The net negatively charged proteins modified through peptide insertions did not adsorb at the hydrophilic and negatively charged silica, irrespective of the peptide insertion, whereas an extensive adsorption was found for the posetively charged DACH surface for all the proteins investigated. For hydrophobic and negatively charged methylated silica, on the other hand, the peptide insertions were found to have a major influence on the protein interfacial behavior, and the adsorption followed the peptide stretch charge, thus increasing in the order ZZNn< ZZTn < ZZPn. These effects are discussed in terms of the relative importance of hydrophobic and electrostatic interactions as driving force for the adsorption.

Place, publisher, year, edition, pages
1998. Vol. 204, 104-111 p.
Keyword [en]
Adsorption, amino acid, ellipsometry, peptide, protein
National Category
Natural Sciences
Identifiers
URN: urn:nbn:se:ri:diva-26725OAI: oai:DiVA.org:ri-26725DiVA: diva2:1053728
Note
A1174Available from: 2016-12-08 Created: 2016-12-08Bibliographically approved

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