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pH-Dependent Interaction between C-Peptide and Phospholipid Bicelles
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
2012 (English)In: Journal of Biophysics, ISSN 1687-8019, 185907- p.Article in journal (Refereed) Published
Abstract [en]

C-peptide is the connecting peptide between the A and B chains of insulin in proinsulin. In this paper, we investigate the interaction between C-peptide and phospholipid bicelles, by circular dichroism and nuclear magnetic resonance spectroscopy, and in particular the pH dependence of this interaction. The results demonstrate that C-peptide is largely unstructured independent of pH, but that a weak structural induction towards a short stretch of β-sheet is induced at low pH, corresponding to the isoelectric point of the peptide. Furthermore, it is demonstrated that C-peptide associates with neutral phospholipid bicelles as well as acidic phospholipid bicelles at this low pH. C-peptide does not undergo a large structural rearrangement as a consequence of lipid interaction, which indicates that the folding and binding are uncoupled. In vivo, local variations in environment, including pH, may cause C-peptide to associate with lipids, which may affect the aggregation state of the peptide.

Place, publisher, year, edition, pages
2012. 185907- p.
National Category
Biophysics
Research subject
Biophysics
Identifiers
URN: urn:nbn:se:su:diva-79050DOI: 10.1155/2012/185907OAI: oai:DiVA.org:su-79050DiVA: diva2:546703
Funder
Swedish Research Council, 621-2011-5964
Available from: 2012-08-24 Created: 2012-08-24 Last updated: 2013-04-29Bibliographically approved
In thesis
1. Membrane Induced Structure in Transmembrane Signaling Proteins and Peptides: Peptide–Lipid Interactions Studied by Spectroscopic Methods
Open this publication in new window or tab >>Membrane Induced Structure in Transmembrane Signaling Proteins and Peptides: Peptide–Lipid Interactions Studied by Spectroscopic Methods
2012 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Biological membranes, defining the boundary of cells and eukaryotic organelles, are mainly composed of lipids and membrane proteins. Interactions between these lipids and proteins are needed to preserve the tight seal of the membrane, but also to induce structure for proper function in many membrane proteins. In this thesis, interactions between three different kinds of peptides, i.e. small proteins, and model membranes are studied by spectroscopic methods.

First, the membrane interaction of two paddle domains, KvAPp, from the voltage-gated potassium channel KvAP from Aeropyrum pernix, and HsapBKp, from the human, large conductance, calcium-activated potassium channel HsapBK, was studied (paper I and II). In paper I, a high-resolution solution NMR structure of HsapBKp in detergent micelles is presented revealing a helix-turn-helix motif. Small structural differences between HsapBKp and KvAPp, positioning the arginines differently, are presented. These structural differences may explain why BK channels are weakly voltage-gated. In paper II, it is shown that HsapBKp perturbs the membrane more than KvAPp and that the membrane perturbation is related to β-structure and to dynamics in the turn in the helix-turn-helix motif.

Second, the membrane interaction of HAMP domains modulating transmission in prokaryotic transmembrane signaling was studied (paper III). Based on the membrane interaction of the AS1 segments of the HAMP domains, two groups were identified: one strongly membrane interacting and one weakly membrane interacting. The two groups are suggested to use different signaling mechanisms.

Third, nonspecific binding of proinsulin C-peptide, the linker peptide connecting chain A and B in insulin, to model membranes was studied (paper IV). The study revealed that C-peptide binds to a model membrane at low pH, but the membrane induces no large structural rearrangements of the peptide. 

Place, publisher, year, edition, pages
Stockholm: Department of Biochemistry and Biophysics, Stockholm University, 2012. 59 p.
Keyword
peptide-lipid interaction, paddle domain, voltage gating, voltage sensor domain, micelle, phospholipid bicelle, solution structure, HAMP domain, nuclear magnetic resonance spectroscopy, circular dichroism spectroscopy, nonspecific interaction
National Category
Biophysics
Research subject
Biophysics
Identifiers
urn:nbn:se:su:diva-79051 (URN)978-91-7447-564-7 (ISBN)
Public defence
2012-09-28, Magnélisalen, Kemiska övningslaboratoriet, Svante Arrhenius väg 16 B, Stockholm, 10:00 (English)
Opponent
Supervisors
Available from: 2012-09-06 Created: 2012-08-24 Last updated: 2012-08-29Bibliographically approved

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