95992-23-7Relevant academic research and scientific papers
Thermodynamic and structural characterization of amino acid-linked dialkyl lipids
Tristram-Nagle, Stephanie,Lewis, Ruthven N.A.H.,Blickenstaff, Joseph W.,DiPrima, Michael,Marques, Bruno F.,McElhaney, Ronald N.,Nagle, John F.,Schneider, James W.
, p. 29 - 39 (2005)
Using differential scanning calorimetry (DSC), X-ray diffraction (XRD) and Fourier transform infrared spectroscopy (FTIR), we determined some thermodynamic and structural parameters for a series of amino acid-linked dialkyl lipids containing a glutamic ac
Synthesis and transfection efficiency of cationic oligopeptide lipids: Role of linker
Gopal, Vijaya,Xavier, Jennifer,Kamal, Md. Zahid,Govindarajan, Srinath,Takafuji, Makoto,Soga, Shuta,Ueno, Takayuki,Ihara, Hirotaka,Rao, Nalam M.
experimental part, p. 2244 - 2254 (2012/04/04)
In the design of new cationic lipids for gene transfection, the chemistry of linkers is widely investigated from the viewpoint of biodegradation and less from their contribution to the biophysical properties. We synthesized two dodecyl lipids with glutami
Thermotropic columnar liquid crystal of a C6-symmetric hydrogen-bonded hexakis(phenylethynyl)benzene derivative with amino acid pendant groups
Sakajiri, Koichi,Yoshida, Hironori,Moriya, Keiichi,Kutsumizu, Shoichi
supporting information; experimental part, p. 1066 - 1067 (2010/06/11)
The thermotropic liquid crystalline Ce-symmetric hydrogen-bonded disk-like molecule has been obtained in a hexakis(phenylethynyl)benzene derivative bearing chiral didodecyl Lglutamates, which forms a hexagonal columnar phase over a wide temperature range
Induction of protein-like molecular architecture by self-assembly processes
Fields, Gregg B.
, p. 75 - 81 (2007/10/03)
One of the most intriguing self-assembly processes is the folding of peptide chains into native protein structures. We have developed a method for building protein-like structural motifs that incorporate sequences of biological interest. A lipophilic moie
Formation of Specific Hydrophobic Sites for Incorporation of Methylene Blue by Laterally Arranged L-Glutamate Residues in Anionic, Crystalline Bilayer Aggregates
Hachisako, Hiroshi,Yamazaki, Tetsuya,Ihara, Hirotaka,Hirayama, Chuichi,Yamada, Kimiho
, p. 1671 - 1680 (2007/10/02)
Bilayer membranes, formed from dioctadecyl L-glutamate-derived anionic amphiphiles, incorporated the cationic dye, methylene blue (MB), into their crystalline, hydrophobic region.The incorporated, monomeric MB was extraordiarily converted into dimeric species during the gel-to-liquid crystalline phase transition by binding to carboxylates.A further increase in temperature upon the phase transition temperature led to the ordinary dimer-to-monomer transition of the bound aggregated MB as well as conventional various dye-polyion systems including micellar systems.However, such extraordinary behaviour strongly depends on the chemical structure of the bilayer-forming component amphiphiles.The molecular structure requirements of anionic amphiphiles for such incorporation has been investigated by varying the alkyl chain length, the average degree of polymerization (x), and the kind of amino acid residue in the connector moiety.Specific incorporation of MB into the crystalline, hydrophobic region is peculiar to molecular assemblies formed from L-glutamte amphiphiles with long alkyl chains and low x values.Corresponding DL-glutamate derivatives showed umbiguous transitions and L-aspartate derivatives did not show such specific incorporation, indicating that the specific behaviour is peculiar to the L-glutamate derivatives.The same conclusion that the monomeric dye species in the crystalline bilayer state is incorporated in the hydrophobic region of the bilayer aggregates could be confirmed by using the solvatochromic dye, 4--N-methylpyridinium iodide (St-4C1), as a microenvironmental probe instead of MB.
