669012-99-1Relevant academic research and scientific papers
Orientation-controlled conjugation of haloalkane dehalogenase fused homing peptides to multifunctional nanoparticles for the specific recognition of cancer cells
Mazzucchelli, Serena,Colombo, Miriam,Verderio, Paolo,Rozek, Ewa,Andreata, Francesco,Galbiati, Elisabetta,Tortora, Paolo,Corsi, Fabio,Prosperi, Davide
supporting information, p. 3121 - 3125 (2013/04/10)
In control: The ligand positioning and orientation on multifunctional nanoparticles (MNP) are controlled by using a versatile bimodular approach that exploits an 11 amino acid (U11) homing peptide genetically fused with a haloalkane dehalogenase (HALO) enzyme. The resultant nanoparticles have good targeting efficiency and selectivity toward broadly occurring urokinase plasminogen activator receptor positive human cancer cells.
The First Direct Evaluation of the Two-Active Site Mechanism for Chitin Synthase
Yeager, Adam R.,Finney, Nathaniel S.
, p. 613 - 618 (2007/10/03)
Chitin synthase polymerizes UDP-GlcNAc to form chitin (poly-β (1,4)-GlcNAc) and is essential for fungal cell wall biosynthesis. The alternating orientation of the GlcNAc residues within the chitin chain has led to the proposal that chitin synthase possesses two active sites. We report the results of the first direct test of this possibility. Two simple uridine-derived dimeric inhibitors are shown to exhibit 10-fold greater inhibition than a monomeric control, consistent with the presence of two active sites. This observation has important implications for the development of antifungal agents, as well as the understanding of polymerizing glycosyltransferases.
