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001-es BibID:	BIBFORM081445
Első szerző:	Bodor Andrea
Cím:	Membrane interactions in small fast-tumbling bicelles as studied by 31P NMR / Andrea Bodor, Katalin E. Kövér, Lena Mäler
Dátum:	2015
ISSN:	0005-2736
Megjegyzések:	Small fast-tumbling bicelles are ideal for studies of membrane interactions at molecular level; they allow analysis of lipid properties using solution-state NMR. In the present study we used 31P NMR relaxation to obtain detailed information on lipid head-group dynamics. We explored the effect of two topologically different membrane-interacting peptides on bicelles containing either dimyristoylphosphocholine (DMPC), or a mixture of DMPC and dimyristoylphosphoglycerol (DMPG), and dihexanoylphosphocholine (DHPC). KALP21 is a model transmembrane peptide, designed to span a DMPC bilayer and dynorphin B is a membrane surface active neuropeptide. KALP21 causes significant increase in bicelle size, as evidenced by both dynamic light scattering and 31P T2 relaxation measurements. The effect of dynorphin B on bicelle size is more modest, although significant effects on T2 relaxation are observed at higher temperatures. A comparison of 31P T1 values for the lipids with and without the peptides showed that dynorphin B has a greater effect on lipid head-group dynamics than KALP21, especially at elevated temperatures. From the field-dependence of T1 relaxation data, a correlation time describing the overall lipid motion was derived. Results indicate that the positively charged dynorphin B decreases the mobility of the lipid molecules - in particular for the negatively charged DMPG - while KALP21 has a more modest influence. Our results demonstrate that while a transmembrane peptide has severe effects on overall bilayer properties, the surface bound peptide has a more dramatic effect in reducing lipid head-group mobility. These observations may be of general importance for understanding peptide?membrane interactions.
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk bicelle Solution31P NMR spectroscopy Relaxation study Membrane protein Dynamic light scattering
Megjelenés:	Biochimica et Biophysica Acta (BBA). Biomembranes. - 1848 : 3 (2015), p. 760-766. -
További szerzők:	Kövér Katalin, E. (1956-2023) (vegyész) Mäler, Lena
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
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