Ennaceur, Sue M., Hicks, Matthew R., Pridmore, Catherine J., Dafforn, Tim, Rodger, Alison and Sanderson, John M.. (2009) Peptide adsorption to lipid bilayers : slow processes revealed by linear dichroism spectroscopy. Biophysical Journal, Vol.96 (No.4). pp. 1399-1407. ISSN 0006-3495

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Abstract

The adsorption and insertion kinetics for the association of two 34-residue cyclic peptides with phosphocholine membranes have been studied using circular and linear dichroism approaches. The two peptides studied are identical with the exception of two residues, which are both tyrosine in one of the peptides and tryptophan in the other. Both peptides adopt random coil conformations in solution in the absence of membranes and do not aggregate at concentrations below 20 PM. After addition to liposome dispersions, circular dichroism spectroscopy indicated that both peptides undergo an extremely rapid transformation to a beta-conformation that remains unchanged throughout the remainder of the experiment. Linear dichroism (LD) spectroscopy was used to study the kinetics of membrane adsorption and insertion. The data were analyzed by nonlinear least squares approaches, leading to identification of a number of bound states and their corresponding LD spectra. Two pseudo-first order processes could be identified that were common to both peptides. The first occurred with a time constant of the order of 1 min and led to a bound state characterized by weak LD signals, with significant bands corresponding to the transitions of aromatic side chains. The second process occurred with an unusually long time constant of between 75 and 100 min, forming a state with considerably stronger positive LD absorbance in the far-ultraviolet region of the spectrum. For the tyrosine-substituted peptide, a third slow process with a long time constant (76 min) could also be delineated and was attributed to rearrangements of the peptide within the membrane.

Item Type:	Journal Article
Subjects:	Q Science > QD Chemistry Q Science > QH Natural history > QH301 Biology Q Science > QP Physiology
Divisions:	Faculty of Science > Chemistry
Library of Congress Subject Headings (LCSH):	Bilayer lipid membranes, Circular dichroism, Membrane proteins, Peptide antibiotics, Amino acids, Tryptophan, Lecithin
Journal or Publication Title:	Biophysical Journal
Publisher:	Biophysical Society
ISSN:	0006-3495
Date:	18 February 2009
Volume:	Vol.96
Number:	No.4
Number of Pages:	9
Page Range:	pp. 1399-1407
Identification Number:	10.1016/j.bpj.2008.10.039
Status:	Peer Reviewed
Publication Status:	Published
Access rights to Published version:	Restricted or Subscription Access
Funder:	Royal Society (Great Britain), Engineering and Physical Sciences Research Council (EPSRC)
Grant number:	RSRG 24281 (RS), GRIT09224/01 (EPSRC)
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URI:	http://wrap.warwick.ac.uk/id/eprint/27916

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