16310-13-7Relevant articles and documents
Identification and quantitation of key aroma compounds formed in Maillard-type reactions of fructose with cysteamine or isothiaproline (1,3-thiazolidine-2-carboxylic acid)
Engel, Wolfgang,Schieberle, Peter
, p. 5394 - 5399 (2002)
Fructose was reacted in the presence of either cysteamine (model A) or isothiaproline (model B) in aqueous buffer at 145 °C and pH 7.0. Application of an aroma extract dilution analysis on the bulk of the volatile compounds formed in model A revealed 5-acetyl-3,4-dihydro-2H-1,4-thiazine (19), N-(2- mercaptoethyl)-1,3-thiazolidine (16), 4-hydroxy-2,5-dimethyl-3(2H)-furanone (15), and 2-acetyl-2- thiazoline (11) as the key aroma compounds among the 10 odorants detected. A similar set of aroma compounds was formed when isothiaproline was reacted (model B), but the flavor dilution factors were generally lower. Substitution of the buffer by silica gel/water (9 + 1 w/w) in both models and application of 150 °C for 10 min also gave the same key odorants from both thio compounds; however, under these conditions isothiaproline was the better precursor of, in particular, 19 and 11. Quantitative measurements performed by means of stable isotope dilution assays revealed a significant effect of the pH on odorant formation. For example, in model A, formation of 19 as well as of 11 was suppressed at pH values 5.0. A clear maximum was, however, found for 19 at pH 7.0 (～1 mol % yield), whereas 11 increased with increasing pH from 7.0 to 9.0.
Preparation of optically active 2-thiazolidinecarboxylic acid by asymmetric transformation
Shiraiwa, Tadashi,Katayama, Takashi,Ishikawa, Joji,Asai, Takeshi,Kurokawa, Hidemoto
, p. 1180 - 1183 (1999)
Cysteamine was condensed with glyoxylic acid monohydrate in a mixture of acetic acid and ethanol in the presence of (2R,3R)- or (2S,3S)-tartaric acid [(R)- or (S)-TA], as the resolving agent, to give the salt of (-)-2- thiazolidinecarboxylic acid [(-)-2-THC] with (R)-TA or the salt of (+)-2-THC with (S)-TA. Treatment of these salts with triethylamine in methanol afforded (-)- and (+)-2-THC. The (-)- and (+)- 2-THC obtained were determined to be enantiopure forms by comparing their powder X-ray diffraction patterns with that of (RS)-2-THC. The absolute configurations of (-)- and (+)-2-THC were estimated based on molar rotations of (2R,4R)- and (2S,4R)-2,4- thiazolidinedicarboxylic acids, (R)-4-thiazolidinecarboxylic acid, and (-)- and (+)-2-THC. ()-2THC was determined to have the (R)-configuration, and (+)- 2-THC to have the (S)-configuration.
BIOCONJUGATION OF POLYPEPTIDES
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Page/Page column 58; 63, (2019/04/26)
Certain embodiments of the present invention relate to methods of forming and manipulating bioconjugates. Particularly, but not exclusively certain embodiments relate to methods of reversible carbon-carbon bond bioconjugation using aldol based chemical reactions at physiological conditions.
Palladium-unleashed proteins: Gentle aldehyde decaging for site-selective protein modification
Brabham, Robin L.,Spears, Richard J.,Walton, Julia,Tyagi, Swati,Lemke, Edward A.,Fascione, Martin A.
supporting information, p. 1501 - 1504 (2018/02/19)
Protein bioconjugation frequently makes use of aldehydes as reactive handles, with methods for their installation being highly valued. Here a new, powerful strategy to unmask a reactive protein aldehyde is presented. A genetically encoded caged glyoxyl aldehyde, situated in solvent-accessible locations, can be rapidly decaged through treatment with just one equivalent of allylpalladium(ii) chloride dimer at physiological pH. The protein aldehyde can undergo subsequent oxime ligation for site-selective protein modification. Quick yet mild conditions, orthogonality and powerful exposed reactivity make this strategy of great potential in protein modification.
Thiazolidine-Masked α-Oxo Aldehyde Functionality for Peptide and Protein Modification
Bi, Xiaobao,Pasunooti, Kalyan Kumar,Lescar, Julien,Liu, Chuan-Fa
, p. 325 - 329 (2017/02/23)
α-Oxo aldehyde-based bioconjugation chemistry has been widely explored in peptide and protein modifications for various applications in biomedical research during the past decades. The generation of α-oxo aldehyde via sodium periodate oxidation is usually limited to the N-terminus of a target protein. Internal-site functionalization of proteins with the α-oxo aldehyde handle has not been achieved yet. Herein we report a novel method for site-specific peptide and protein modification using synthetically or genetically incorporated thiazolidine-protected α-oxo aldehyde. Efficient unmasking of the aldehyde was achieved by silver ion-mediated hydrolysis of thiazolidine under mild conditions for the first time. A model peptide and a recombinant protein were used to demonstrate the utility of this new method, which were site-specifically modified by oxime ligation with an oxyamine-functionalized peptide labeling reagent. Therefore, our current method has enriched the α-oxo aldehyde synthetic tool box in peptide and protein bioconjugation chemistry and holds great potential to be explored in novel applications in the future.
Anti-heparin peptides
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, (2008/06/13)
The invention concerns a compound exhibiting an anti-heparin activity, of formula Z Bm ! (AXA)x Bn ! (AXA)y Bo (AXA)z Bp, the diagnostic reagents comprising it and the use of said compound in an in vitro diagnostic test of a medicine for anti-heparin activity.
Synthesis and antineoplastic activity of 5-aryl-2,3-dihydropyrrolo[2,1-b]thiazole-6,7-dimethanol 6,7-bis-(isopropylcarbamates)
Lalezari,Schwartz
, p. 1427 - 1429 (2007/10/02)
A series of 1-thia analogues of the pyrrolizine bis(carbamate) 9 (NSC-278214), namely 5-aryl-2,3-dihydropyrrolo-[2,1-b]thiazole-6,7-dimethanol 6,7-bis(isopropylcarbamates) (7a-d), were prepared by multistep syntheses from the proline analogues thiazolidin
Fungicidal 6-(3,5-dichlorophenyl)perhydroimidazo[5,1-b]thiazole derivatives
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, (2008/06/13)
This invention relates to fungicidal novel derivatives of 6-(3,5-dichlorophenyl)perhydroimidazo[5,1-b]thiazole derivative. These compounds may be used for controlling fungal infection, especially in agriculture.
Study of the structural requirements for dopa potentiation and oxotremorine antagonism by L-propyl-L-leucylglycinamide
Johnson,Smissman
, p. 165 - 169 (2007/10/04)
A number of analogues of the tripeptide L-prolyl-L-leucylglycinamide (1) were synthesized and evaluated in the Dopa potentiation and oxotremorine antagonism tests. The replacement of the glycinamide residue with either the glycine methylamide, glycine, aminoacetronitrile, amino-2-propanone, semicarbazide, or β-alaninamide residues resulted in a loss of activity in both tests. A 1:1 mixture of L-prolyl-L-leucyl-(-)-thiazolidine-2-carboxamide and L-propyl-L-leucyl-(+)-thiazolidine-2-carboxamide showed marked activity in the Dopa potentiation test but was unable to antagonize the tremors induced by oxotremorine. L-prolyl-L-leucyl-L-prolinamide, on the other hand, was active in the oxotremorine antagonism test but inactive in the Dopa potentiation test. The replacement of the pyrrolidine ring of 1 with either a thiazolidine or cyclopentane ring system caused a loss of activity. The cyclopentanecarboxylic acid analogue 13, however, was found to have moderate activity in the serotinin potentiation test.
