1111765-75-3Relevant academic research and scientific papers
CYCLIC AZAPEPTIDES AS INTEGRIN MARKERS
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Paragraph 0094, (2015/09/28)
The present application is directed to radiolabeled cyclic polyazapeptides, pharmaceutical compositions comprising radiolabeled cyclic polyazapeptides, and methods of using the radiolabeled cyclic polyazapeptides. Such polyazapeptides can be used in imaging studies, such as Positron Emitting Tomography (PET) or Single Photon Emission Computed Tomography (SPECT).
Cyclic aza-peptide integrin ligand synthesis and biological activity
Spiegel, Jochen,Mas-Moruno, Carlos,Kessler, Horst,Lubell, William D.
experimental part, p. 5271 - 5278 (2012/09/25)
Aza-peptides are obtained by replacement of the α-C-atom of one or more amino acids by a nitrogen atom in a peptide sequence. Introduction of aza-residues into peptide sequences may result in unique structural and pharmacological properties, such that aza-scanning may be used to probe structure-activity relationships. In this study, a general approach for the synthesis of cyclic aza-peptides was developed by modification of strategies for linear aza-peptide synthesis and applied in the preparation of cyclic aza-pentapeptides containing the RGD (Arg-Gly-Asp) sequence. Aza-amino acid scanning was performed on the cyclic RGD-peptide Cilengitide, cyclo[R-G-D-f-N(Me)V] 1, and its parent peptide cyclo(R-G-D-f-V) 2, potent antagonists of the αvβ3, αvβ5, and α5β1 integrin receptors, which play important roles in human tumor metastasis and tumor-induced angiogenesis. Although incorporation of the aza-residues resulted generally in a loss of binding affinity, cyclic aza-peptides containing aza-glycine retained nanomolar activity toward the αvβ3 receptor.
Azapeptide analogues of the growth hormone releasing peptide 6 as cluster of differentiation 36 receptor ligands with reduced affinity for the growth hormone secretagogue receptor 1a
Proulx, Caroline,Picard, émilie,Boeglin, Damien,Pohankova, Petra,Chemtob, Sylvain,Ong, Huy,Lubell, William D.
scheme or table, p. 6502 - 6511 (2012/10/08)
The synthetic hexapeptide growth hormone releasing peptide-6 (GHRP-6) exhibits dual affinity for the growth hormone secretagogue receptor 1a (GHS-R1a) and the cluster of differentiation 36 (CD36) receptor. Azapeptide GHRP-6 analogues have been synthesized, exhibiting micromolar affinity to the CD36 receptor with reduced affinity toward the GHS-R1a. A combinatorial split-and-mix approach furnished aza-GHRP-6 leads, which were further examined by alanine scanning. Incorporation of an aza-amino acid residue respectively at the d-Trp2, Ala3, or Trp4 position gave aza-GHRP-6 analogues with reduced affinity toward the GHS-R1a by at least a factor of 100 and in certain cases retained affinity for the CD36 receptor. In the latter cases, the d-Trp2 residue proved important for CD36 receptor affinity; however, His1 could be replaced by Ala1 without considerable loss of binding. In a microvascular sprouting assay using a choroid explant, [azaTyr4]-GHRP-6 (15), [Ala1, azaPhe 2]-GHRP-6 (16), and [azaLeu3, Ala6]-GHRP-6 (33) all exhibited antiangiogenic activity.
Solvent-free synthesis of hydrazones and their subsequent N-alkylation in a Ball-mill
Nun, Pierrick,Martin, Charlotte,Martinez, Jean,Lamaty, Frédéric
, p. 8187 - 8194 (2011/10/31)
A large variety of Boc-, Bz-, Ts-, and Fmoc- protected hydrazones were prepared via condensation of an equimolar amount of carbonyl-compound and the corresponding hydrazine using a ball-mill. Hydrazones were always obtained in a quantitative yield and no solvents were used at any step. In a second step, we realized the first solvent-free N-allylation and N-benzylation of these hydrazones.
