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Peptide adsorption to lipid bilayers : slow processes revealed by linear dichroism spectroscopy
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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. doi:10.1016/j.bpj.2008.10.039 ISSN 0006-3495.
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Official URL: http://dx.doi.org/10.1016/j.bpj.2008.10.039
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 | ||||
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Subjects: | Q Science > QD Chemistry Q Science > QH Natural history > QH301 Biology Q Science > QP Physiology |
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Divisions: | Faculty of Science, Engineering and Medicine > 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 | ||||
Official Date: | 18 February 2009 | ||||
Dates: |
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Volume: | Vol.96 | ||||
Number: | No.4 | ||||
Number of Pages: | 9 | ||||
Page Range: | pp. 1399-1407 | ||||
DOI: | 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) |
Data sourced from Thomson Reuters' Web of Knowledge
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