2875-41-4Relevant academic research and scientific papers
Interaction of Poly and Its Derivatives with Lipid Membrane
Yagi, Yoshiko,Kimura, Shunsaku,Imanishi, Yukio
, p. 3983 - 3990 (1988)
Poly (PolyNAPGly, 5) and its derivatives were synthesized as a model peptides of the membrane-bound enzymes, and investigated on their interactions with lipid membrane.PolyNAPGly (5) was shown to be distributed to dipalmitoylphosphatidyl choline biolayer membrane without destruction of the vesicle structure.Dodecyl groups were introduced to the side chains of PolyNAPGly (5), and found to facilitate binding of the polymer to lipid membrane.However, the introduction of the excess amount of hydrophobic groups to PolyNAPGly (5) caused the formation of polymer micelles, and the addition of such polymers to lipid vesicles destroyed the membrane structure.The derivative of PolyNAPGly (5) (n=35) bearing one or two dodecyl groups and some N'-benzyloxycarbonylhistidyl groups was found to be bound tightly to lipid membrane without destruction of the membrane structure.The addition of these polypeptides to vesicles decreased the membrane fluidity.
SYNTHESIS OF CYCLOCREATINE AND ANALOGS THEREOF
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Paragraph 0046, (2016/09/26)
Provided herein is a process and intermediates for the preparation of a compound of formula (I): or a pharmaceutically acceptable salt thereof, using cyanamide in the reaction.
Building Units for N-Backbone Cyclic Peptides. 1. Synthesis of Protected N-(ω-Aminoalkylene)amino Acids and Their Incorporation into Dipeptide Units
Byk, Gerardo,Gilon, Chaim
, p. 5687 - 5692 (2007/10/02)
A variety of new amino acids which contain an ω-aminoalkylene group on the Nα-amino nitrogen were synthesized by alkylation of alkylenediamines with α-halogeno acids.The reaction proceeds with inversion of configuration; thus, optically pure products were obtained when optically active α-halogeno acids were used.The N-(ω-aminoalkylene)amino acids were protected by orthogonal protecting groups to allow their incorporation into dipeptides by the "solution" techniques and into peptides by the solid-phase peptide synthesis (SPPS) methodology.A series of dipeptide analogs of Phe-Gly, Leu-Gly, Trp-Gly, Phe-Leu, and Phe-Ala in which the nitrogen of the peptide bond is alkylated by ω-aminoalkylene chains with various lengths were prepared.These new protected N-(ω-aminoalkylene)amino acids and their derived dipeptide units may be used as building blocks for conformationally constrained N-backbone cyclic peptides.
