Disease relevance of D-Trytophane

• Role of D-tryptophan oxidase in D-tryptophan utilization by Escherichia coli [1].
• Effect of D-tryptophan on hemolysin production in Vibrio parahaemolyticus [2].
• Conversion of D-tryptophan to the L-isomer in the rat was found by an examination of plasma from the posterior vena cava and the portal vein, following stomach intubation of 100 micromoles D-tryptophan/100 g of body weight [3].
• Indole and 7-derivatives, L- and D-tryptophan and 9 derivatives, and beta-carboline (norharman) and 11 derivatives were tested for mutagenicity to Salmonella typhimurium TA100 and TA98 after nitrite treatment [4].
• In BQ123 the fluorescence characteristics support the occurrence of a dominant rotameric form involving the indole sidechain of the D-tryptophan residue (C alpha-C beta torsion angle chi 1 of 60 degrees, as previously determined by NMR [5].

High impact information on D-Trytophane

• Addition of L-tryptophan, but not other aromatic amino acids, other essential amino acids, or D-tryptophan, prevented inhibition of cell growth by IFN-gamma [6].
• Hexarelin, an analogue of GHRP-6, in which D-Tryptophan has been replaced by its 2-methyl derivative, is known to release growth hormone (GH) in vivo and in vitro by direct action on receptors present in anterior pituitary cells [7].
• The introduction of D-tryptophan analogues with C-2 substituents in these peptidic ET antagonists resulted in potent ET receptor antagonists with various ETA/ETB subtype selectivity [8].
• Synthesis and structure-activity relationships of 2-substituted D-tryptophan-containing peptidic endothelin receptor antagonists: importance of the C-2 substituent of the D-tryptophan residue for endothelin A and B receptor subtype selectivity [8].
• Replacing the tryptophan by a D-tryptophan in such analogs produced full CCK-receptor antagonists [9].

Chemical compound and disease context of D-Trytophane

• Mutants of Escherichia coli K-12 that require L-tryptophan (trp) are normally unable to utilize D-tryptophan to fulfill their requirement [1].

Biological context of D-Trytophane

• Studies on structure-activity relationships revealed that the D-tryptophan, L-phenylalanine, and benzyl ester were quite important to maintain the high binding affinity [10].
• The nutritive values of DL- and D-tryptophan relative to the L-isomer were 47 and 21%, respectively in chicks and close to 100% in rats [11].
• Using a chemically defined amino acid diet that was singly deficient in tryptophan, bioavailability of tryptophan was determined for casein, fresh TwoCal-HN, expired TwoCal-HN and D-tryptophan [12].
• The amino acid sequence of Contryphan-Vn is As with other contryphans, Contryphan-Vn contains a d-tryptophan residue, is amidated at the C-terminus, and maintains the five-residue intercystine loop size [13].
• BACKGROUND: L-Tryptophan delays gastric emptying in animals to a greater extent than D-tryptophan, but none of the possible motor mechanisms responsible for this stereospecific effect have been evaluated [14].

Anatomical context of D-Trytophane

• Formation of D-myo-inositol 1,4,5-trisphosphate (IP3) in melanophores was reduced (15-58%, no concentration dependence) by saccharin, D-tryptophan, and cyclo(Leu-Trp) stimulation but increased by NHD stimulation [15].
• The amphids were stimulated by blood serum from a host bird and by D-tryptophan [16].

Associations of D-Trytophane with other chemical compounds

• Cyclic peptides containing a D-phenylalanine and a D-tryptophan residue have been synthesized and tested as inhibitors of human renin [17].
• CTA was achieved by injecting LiCl after drinking glycine, and next its generalization to 10 taste solutions (glycine, sucrose, saccharin, D-tryptophan, L-tryptophan, L-alanine, L-proline, L-glutamine, NaCl, and HCl) was examined by video recording licking behavior [18].
• The classical approach used in the development of substance P (SP) antagonists, i.e. the introduction of multiple D-tryptophan (D-Trp), was successfully extended to neurokinin A (NKA) [19].
• This enzyme utilizes the superoxide anion (O2-) as a substrate for the oxidation of either L- or D-tryptophan to N-formylkynurenic acid leading to cell death [20].
• No difference within the experimental error (approximately 10(-3)) was observed in the absorption of right- and left-circularly polarized gamma-radiation in L- and D-tryptophan and tyrosine [21].

Gene context of D-Trytophane

• A highly selective NK-2 tachykinin receptor antagonist containing D-tryptophan [19].
• Synthesis and biological activity of NK-2 selective tachykinin antagonists containing D-tryptophan [22].
• The D-tryptophan analog was less effective than native SRIF [23].
• The cytotoxicity of gamma-IFN and TNF-alpha could be reversed in all cells by the addition of L- or D-tryptophan to the culture medium [20].
• Upon the addition of single amino acids to this synthetic medium, only D-tryptophan induced production of the hemolysin [24].

Analytical, diagnostic and therapeutic context of D-Trytophane

• The occurrence of a D-tryptophan residue was confirmed by chemical synthesis and HPLC elution profiles [25].
• The dog appears to be a reasonable animal model for the human in studies of D-tryptophan metabolism [26].
• D-Tca-Cys-Tyr-D-Trp-Arg-Thr-Pen-Thr-NH2 ([D-Tca1]CTAP) (where D-Tca is a cyclic D-tryptophan analogue) was synthesized and evaluated in radioligand competition assays, opioid bioassays, and in an antinociceptive assay (the tail-flick test in mice) [27].
• Ultraviolet resonance Raman spectroscopy demonstrates a difference in the D-tryptophan dihedral angle for the two contryphan-Tx equilibrium conformers [28].

References