A designed buried salt bridge modulates heterodimerization of a membrane peptide
| Autor: | Bhupesh Goyal, Marcia Levitus, Sandip Shinde, Giovanna Ghirlanda, Jennifer K. Binder, Brian W. Woodrum, Sonia De Munari |
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| Rok vydání: | 2014 |
| Předmět: |
Stereochemistry
Carboxylic acid Molecular Sequence Data Biophysics Peptide Biochemistry Micelle Protein Structure Secondary Biomaterials Fluorescence Resonance Energy Transfer Amino Acid Sequence chemistry.chemical_classification Chemistry Organic Chemistry Cell Membrane General Medicine Salt bridge (protein and supramolecular) Hydrogen-Ion Concentration Transmembrane protein Membrane Förster resonance energy transfer Membrane protein Electrophoresis Polyacrylamide Gel Salts Protein Multimerization Peptides |
| Zdroj: | Biopolymers. 102(6) |
| ISSN: | 1097-0282 |
| Popis: | Specific helix–helix interactions underpin the correct assembly of multipass membrane proteins. Here, we show that a designed buried salt bridge mediates heterodimer formation of model transmembrane helical peptides in a pH-dependent manner. The model peptides bear side chains functionalized with either a carboxylic acid or a primary amine within a hydrophobic segment. The association behavior was monitored by Forster resonance energy transfer, revealing that heterodimer formation is maximized at a pH close to neutrality (pH 6.5), at which each peptide is found in a charged state. In contrast, heterodimerization is disfavored at low and high values of pH, because either the carboxylic acid or the primary amine is present in its neutral state, thus preventing the formation of a salt bridge. These findings provide a blueprint for the design and modulation of protein–protein interactions in membrane proteins. © 2014 Wiley Periodicals, Inc. Biopolymers (Pept Sci) 102: 437–443, 2014. |
| Databáze: | OpenAIRE |
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