What's new for 'Trypanosomatids' in PubMed

This message contains My NCBI what's new results from the National Center for Biotechnology Information (NCBI) at the U.S. National Library of Medicine (NLM).
Do not reply directly to this message.

Sender's message:

Sent on Thursday, 2009 Nov 12
Search kinetoplastids OR kinetoplastid OR Kinetoplastida OR "trypanosoma brucei" OR leishmania OR brucei OR leishmaniasis OR "African trypanosomiasis"
Click here to view complete results in PubMed. (Results may change over time.)
To unsubscribe from these e-mail updates click here.

PubMed Results

Items 1 -2 of 2

1.	AAPS PharmSciTech. 2009 Nov 11. [Epub ahead of print] Uptake of Biodegradable Gel-Assisted LBL Nanomatrix by Leishmania donovani-Infected Macrophages. Gupta GK, Kansal S, Misra P, Dube A, Mishra PR. Pharmaceutics Division, Central Drug Research Institute, Chattar Manzil Palace, P.O. Box 173, Lucknow, UP, 226001, India. The aim of this study was to develop novel gel-assisted layer-by-layer (LBL) nanomatrix with high payload of doxorubicin (DOX) and to assess its efficacy against Leishmania donovani. The biodegradable LBL nanomatrix was fabricated using LBL technique using polyions (protamine and sodium alginate) on decomposable core. The developed system was characterized in vitro in terms of layer-by-layer growth and payload efficiency. The efficacy of optimized formulations was evaluated against L. donovani strain in terms of inhibitory concentration (IC(50)). Uptake studies by infected macrophages were investigated both qualitatively and quantitatively using fluorescence microscopy and flow cytometry. The autogelling property subsequent to core removal inside the nanomatrix resulted in high payload efficiency of DOX (i.e., >70%). The reversal in charge followed the same trend with additional layers, and the magnitude of the charge remained constant up to five complete bilayers of polyions. The DOX can be effectively encapsulated, delivered, and subsequently taken up by L. donovani-infected macrophage cells. The matrix is completely internalized into macrophages showing improved efficacy (IC(50) of formulation is almost </=1.9-fold as compared to plain drug, P < 0.05) against intracellular amastigotes. Having ample of opportunity to manipulate surface architecture, this system demonstrates unique platform as a low cost ideal substitute for visceral leishmaniasis to expensive lipid-based formulations.
	PMID: 19904614 [PubMed - as supplied by publisher]
	Related articles

2.	Comp Biochem Physiol B Biochem Mol Biol. 2009 Nov 7. [Epub ahead of print] A lactose specific lectin from the sponge Cinachyrella apion: Purification, characterization, N-terminal sequences alignment and agglutinating activity on Leishmania promastigotes. Medeiros DS, Medeiros TL, Ribeiro JK, Monteiro NK, Migliolo L, Uchoa AF, Vasconcelos IM, Oliveira AS, de Sales MP, Santos EA. Departamento de Bioquímica, Centro de Biociências, Universidade Federal do Rio Grande do Norte, Natal, RN, Brazil. Crude extract from the sponge Cinachyrella apion showed cross-reactivity with the polyclonal antibody IgG anti-CvL (Cliona varians lectin) and also a strong haemmaglutinating activity towards human erythrocytes of all ABO groups. Thus, it was submitted to acetone fractionation, IgG anti-deglicosilated CvL Sepharose affinity chromatography, and Fast Protein Liquid Chromatography (FPLC-AKTA Purifier) gel filtration on a Superose 6 10/300 column to purify a novel lectin. C. apion lectin (CaL) agglutinated all types of human erythrocytes with preference for papainized type A erythrocytes. The haemagglutinating activity is independent of Ca(2+), Mg(2+) and Mn(2+) ions, and it was strongly inhibited by the disaccharide lactose, up to a minimum concentration of 6.25mM. CaL molecular mass, determined by FPLC-gel filtration on a Superose 12 10/300 column and SDS gel electrophoresis, was approximately 124kDa, consisting of eight subunits of 15,5kDa, assembled by hydrophobic interactions. The lectin was heat-stable between 0 and 60 degrees C and pH-stable. The N-terminal amino acid sequence of CaL was also determined and a blast search on amino acid sequences revealed that the protein showed similarity only with a silicatein. Leishmania chagasi promastigotes were agglutinated by CaL and this activity was abolished by lactose, indicating that lactose receptors could be presented in this parasite stage. These findings are indicative of the potential biotechnological application of CaL as diagnostic of pathogenic protozoa.
	PMID: 19903536 [PubMed - as supplied by publisher]
	Related articles