Related ArticlesConformational Plasticity of the Cell-Penetrating Peptide SAP As Revealed by Solid-State 19F-NMR and Circular Dichroism Spectroscopies.
J Phys Chem B. 2017 07 13;121(27):6479-6491
Authors: Afonin S, Kubyshkin V, Mykhailiuk PK, Komarov IV, Ulrich AS
Abstract
The cell-penetrating peptide SAP, which was designed as an amphipathic poly-l-proline helix II (PPII), was suggested to self-assemble into regular fibrils that are relevant for its internalization. Herein we have analyzed the structure of SAP in the membrane-bound state by solid-state 19F-NMR, which revealed other structural states, in addition to the expected surface-aligned PPII. Trifluoromethyl-bicyclopentyl-glycine (CF3-Bpg) and two rigid isomers of trifluoromethyl-4,5-methanoprolines (CF3-MePro) were used as labels for 19F-NMR analysis. The equilibria between different conformations of SAP were studied and were found to be shifted by the substituents at Pro-11. Synchrotron-CD results suggested that substituting Pro-11 by CF3-MePro governed the coil-to-PPII equilibrium in solution and in the presence of a lipid bilayer. Using CD and 19F-NMR, we examined the slow kinetics of the association of SAP with membranes and the dependence of the SAP conformational dynamics on the lipid composition. The peptide did not bind to lipids in the solid ordered phase and aggregated only in the liquid ordered "raft"-like bilayers. Self-association could not be detected in solution or in the presence of liquid disordered membranes. Surface-bound amphipathic SAP in a nonaggregated state was structured as a mixture of nonideal extended conformations reflecting the equilibrium already present in solution, i.e., before binding to the membrane.
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Abstract
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Abstract
A new class of penetrating peptides that can target the mitochondria with high specificity was recently discovered. In this work, we...
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The interaction of thiocyanate with human native and cross-linked...
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Biochemistry. 1991 Oct 1;30(39):9387-95
Authors: Atkinson RA, Saudek V, Huggins JP, Pelton JT
Cyclic GMP dependent protein kinase exists as a dimer in its native form. A peptide corresponding to the dimerization domain in the N-terminal segment has been characterized...
Conformational Plasticity of the Cell-Penetrating Peptide SAP As Revealed by Solid-State 19F-NMR and Circular Dichroism Spectroscopies.
Linear Mode
