407629-42-9Relevant academic research and scientific papers
COMPOSITIONS AND METHODS FOR SYNTHETIC AMPHIPHILE-INDUCED CHANGES IN PLANT ROOT MORPHOLOGY
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Paragraph 0123, (2016/04/04)
The disclosure provides a method for increasing the lateral root development of a plant by exposing said plant to a composition containing a synthetic amphiphile. By increasing the number of lateral roots, the surface area of the root structure is increased, making the plants better able to survive such stresses as drought or low nutrients
The effect of midpolar regime mimics on anion transport mediated by amphiphilic heptapeptides
Pajewski, Robert,Pajewska, Jolanta,Li, Ruiqiong,Daschbach, Megan M.,Fowler, Elizabeth A.,Gokel, George W.
, p. 1960 - 1972 (2008/03/14)
Nine amphiphilic heptapeptides, synthetic anion transporters (SATs) of the form (C18H37)2N-Y-(Gly)3-Pro-(Gly) 3-OCH2Ph were prepared. The unit (OH2)Y represents the diacids succi
Cation dependence of chloride ion complexation by open-chained receptor molecules in chloroform solution
Pajewski, Robert,Ferdani, Riccardo,Pajewska, Jolanta,Li, Ruiqiong,Gokel, George W.
, p. 18281 - 18295 (2007/10/03)
Seventeen peptides, most having the sequence GGGPGGG, but differing in the C- and N-terminal ends, have been studied as anion-complexing agents. These relatively simple, open-chained peptide systems interact with both chloride and the associated cation. Changes in the N- and C-terminal side chains appear to make little difference in the efficacy of binding. NMR studies suggest that the primary interactions involve amide NH contacts with the chloride anion, and CD spectral analyses suggest a concomitant conformational change upon binding. Changes in binding constants, which are expected in different solvents, also suggest selective solvent interactions with the unbound host that helps to preorganize the open-chained peptide system. Significant differences are apparent in complexation strengths when the heptapeptide chain is shortened or lengthened or when the relative position of proline within the heptapeptide is varied.
Replacing proline at the apex of heptapeptide-based chloride ion transporters alters their properties and their ionophoretic efficacy
Schlesinger, Paul H.,Ferdani, Riccardo,Pajewska, Jolanta,Pajewski, Robert,Gokel, George W.
, p. 60 - 67 (2007/10/03)
A membrane anchored heptapeptide, (C18H37)2NHCOCH2OCH 2CO-NH-Gly-Gly-Gly-Pro-Gly-Gly-Gly-OCH2Ph, has proved to be a selective chloride anion transporter that functions in phospholipid bilay
Anchor chain length alters the apparent mechanism of chloride channel function in SCMTR derivatives
Schlesinger, Paul H.,Djedovic, Natasha K.,Ferdani, Riccardo,Pajewska, Jolanta,Pajewski, Robert,Gokel, George W.
, p. 308 - 309 (2007/10/03)
Two membrane-anchored heptapeptides have been prepared and their pore-formation behavior in phospholipid bilayer membranes has been found to differ profoundly as a result only of alkyl chain length.
SCMTR: A chloride-selective, membrane-anchored peptide channel that exhibits voltage gating
Schlesinger, Paul H.,Ferdani, Riccardo,Liu, Jun,Pajewska, Jolanta,Pajewski, Robert,Saito, Mitsuyoshi,Shabany, Hossein,Gokel, George W.
, p. 1848 - 1849 (2007/10/03)
The design, synthesis, and characterization of a synthetic chloride membrane transporter, SCMTR (synthetic chloride membrane transporter, "scimitar"), are presented. The compound [CH3(CH2)17]2NCOCH2OC
The L-Proline Residue as a 'Break-point' in Metal - Peptide Systems
Pettit, Leslie D.,Steel, Ian,Formicka-Kozlowska, Grazyna,Tatarowski, Tomasz,Bataille, Michael
, p. 535 - 540 (2007/10/02)
Results are reported of a potentiometric and spectrophotometric study of the H+ and Cu2+ complexes of the tetrapeptides X-Gly-Gly-Gly, Gly-X-Gly-Gly, Gly-Gly-X-Gly, and Gly-Gly-Gly-X where X is the proline (Pro) and sarcosine (Sar) residue (Gly=glycine).All the tetrapeptides (HL) form the series of complexes , -1L>, -2L>, and -3L> (charges omitted).The ligands Gly-X-Gly-Gly also form the bis-complex, .When inserted in a peptide chain the Pro and Sar residues cannot co-ordinate to Cu2+ through their peptide nitrogens since they do not possess ionizable protons.In addition the Pro residue tends to force the peptide chain to form a 'β-turn' and so adopt a 'bent' conformation.These studies demonstrate the formation of a large chelate ring when tetrapeptides containing Pro (and , to a smaller extent, Sar) in the second or third positions co-ordinate to Cu2+.This ring spans the terminal residues of the peptide chain and locks the peptide into a 'bent' or 'horse-shoe' shaped conformation.Cu2+ could therefore play an important role in activating oligopeptides (e.g. neuropeptides) containing proline.
