uu.seUppsala University Publications
Change search
ReferencesLink to record
Permanent link

Direct link
Investigation of the adsorption behavior of glycine peptides on 12% cross-linked agarose gel media
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry.
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Physical and Analytical Chemistry.
Show others and affiliations
2010 (English)In: Journal of Chromatography A, ISSN 0021-9673, E-ISSN 1873-3778, Vol. 1217, no 12, 1916-1925 p.Article in journal (Refereed) Published
Abstract [en]

The highly cross-linked 12% agarose gel Superose 12 10/300 GL Causes retardation of glycine peptides when mobile phases containing varying concentrations of acetonitrile in water are used An investigation has been made into the retention mechanism behind this retardation using the glycine dipeptide (GG) and tripeptide (GGG) as models The dependence of retention times of analytical-size peaks Under different experimental conditions was interpreted such that the adsorption most probably was caused by the formation of hydrogen bonds but that electrostatic interactions cannot be ruled Out Thereafter, a nonlinear adsorption study Was undertaken at different acetonitrile content in the eluent, using the elution by characteristic points (ECPs) method on strongly overloaded GG and GGG peaks With a new evaluation tool, the adsorption energy distribution (AED) Could be calculated prior to the model selection These calculations revealed that when the acetonitrile content in the eluent was varied from 0% to 20% the interactions turned from (i) being homogenous (GG) or mildly heterogeneous (GGG), (ii) via a more or less stronger degree of heterogeneity around one site to (iii) finally a typical bimodal energy interaction comprising of two sites (GG at 20% and GGG at 10% and 20%) The Langmuir, Toth and bi-Langmuir models described these interesting adsorption trends excellently Thus, the retardation observed for these glycine peptides is interpreted as being of mixed-mode character composed of electrostatic bonds and hydrogen bonds.

Place, publisher, year, edition, pages
2010. Vol. 1217, no 12, 1916-1925 p.
Keyword [en]
Superose 12 10/300 GL, Peptides, Adsorption isotherms, Adsorption energy distribution, Heterogeneous interaction, Hydrogen bond formation, Langmuir model, Toth model, bi-Langmuir model, Mixed mode, Electrostatic interactions
National Category
Chemical Sciences
URN: urn:nbn:se:uu:diva-136805DOI: 10.1016/j.chroma.2010.01.058ISI: 000275680600008PubMedID: 20167326OAI: oai:DiVA.org:uu-136805DiVA: diva2:377520
Available from: 2010-12-14 Created: 2010-12-14 Last updated: 2010-12-14Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full textPubMed
By organisation
Department of Physical and Analytical Chemistry
In the same journal
Journal of Chromatography A
Chemical Sciences

Search outside of DiVA

GoogleGoogle Scholar
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

Altmetric score

Total: 144 hits
ReferencesLink to record
Permanent link

Direct link