80165-23-7Relevant academic research and scientific papers
Preparation and preliminary biological evaluation of 177Lu- labeled GluDTPA-cyclo(RGDfK) for integrin αvβ3 receptor-positive tumor targeting
Kim, Jin-Hwan,Lim, Jae-Cheong,Yun, Ki-Cheol,Choi, Sun-Ju,Hong, Young-Don
experimental part, p. 10 - 17 (2012/06/30)
Integrin αvβ3 is a receptor and is highly expressed on activated and proliferating endothelial cells during the growth and metastasis of solid tumors but not on resting endothelial cells and normal organs. Because RGD peptide binds to integrin αvβ 3 receptor, a variety of radiolabeled RGD peptides have been evaluated for non-invasive imaging of integrin αvβ 3-positive tumors. In an attempt to develop RGD-based radiopharmaceuticals, a novel GluDTPA-cyclo arginine-glycine-aspartic acid-d-phenylalanine-lysine (GluDTPA-cycloRGDfK) was simply synthesized and radiolabeled with 177Lu. Also, tumor targeting and retention of the radiolabeled complex were evaluated in U87MG glioma-bearing mice. The 177Lu-labeled GluDTPA-cyclo(RGDfK) was formulated with a high radiolabeling yield (>98%) under mild condition, and the radiochemical purity was sustained in both saline and serum for over 4days at 37°C. The radiolabeled compounds were rapidly cleared from the blood pool and non-target tissue. Tumor-to-blood ratio was 12.09 at 2h post injection and increased to 134.67 at 24h, while tumor to liver ratio was 2.01 at 24h similar to that of 2h. Though it is inappropriate for targeted therapy due to its low uptake in tumor (～ 1 %ID/g), the acceptable results on radiochemistry and biodistribution propose to take a further assessment for non-invasive imaging and detection of integrin αvβ3-positive tumors by applying diagnostic radionuclides.
The in vitro transport of model thiodipeptide prodrugs designed to target the intestinal oligopeptide transporter, PepT1
Foley, David,Pieri, Myrtani,Pettecrew, Rachel,Price, Richard,Miles, Stephen,Lam, Ho Kam,Bailey, Patrick,Meredith, David
supporting information; experimental part, p. 3652 - 3656 (2009/10/23)
A thiodipeptide carrier system is shown to be effective at enabling a range of covalently bound molecules, including benzyl, benzoyl and ibuprofen conjugates, to be transported via the intestinal peptide transporter PepT1, demonstrating its potential as a rational drug delivery target.
Chemoselective deprotection of N-Boc group in amino acids and peptides by bismuth(III) trichloride
Navath, Raghavendra S.,Pabbisetty, Kumar B.,Hu, Longqin
, p. 389 - 393 (2007/10/03)
Selective deprotection of N-Boc group was achieved in excellent yields using bismuth(III) trichloride in a mixed solvent of acetonitrile and water (50:1, v/v) at 55°C. Acid-labile groups such as Pmc and tert-butyl ester were not affected and no alkylation of tryptophan, methionine, and cysteine residues was observed under the deprotection conditions.
The synthesis of pyrimidin-4-yI substituted a-amino acids. a versatile approach from alkynyl ketones
Adlington, Robert M.,Baldwin, Jack E.,Catterick, David,Pritchard, Garcth J.
, p. 855 - 866 (2007/10/03)
The reaction of amidines with a-amino acid alkynyl ketones is shown to be a versatile route to pyrimidin-4-yl substituted a-amino acids. This route is also applicable to a parallel synthesis approach and has allowed the formation of a range of pyrimidin-4-yl substituted a-amino acids, including the naturally occurring a-amino acid L-lathyrine 4.
