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41.
A.?GraffEmail author D.?Tropel SK.?Raman G.?Machaidze U.?Aebi P.?BurkhardEmail author 《NanoBioTechnology》2005,1(3):293-294
A challenging topic in cancer research is to create drug delivery system that can bring in a specific and noncytotoxic manner
a therapeutic compound. Usually, tumor targeting requires very specific compounds. Currently, peptide analogues like somatostatin,
neurotensin, or bombesin are used to target G-coupled receptors, which are overexpressed on tumor cells. However, many of
those analogues are rapidly degraded in the plasma and are cytotoxic [1–2]. Due to the limited efficiency and high toxicity
of conventional chemotherapy different strategies have been developed for non-cytotoxic cancer treatment and cancer localization
[3–5].
The recent development in bio-nanotechnology offers new avenues for cancer therapy. A lot of studies have been devoted to
nanoparticulate delivery systems (10–100nm) like lipid or polymer particles [6–8]. Due to the nanometer sized of such cargos,
the transportation of therapeutic compounds in the blood stream is increased in terms of time circulation. But their surface
functionalization to improve drug-targeting properties is usually complicated and rather uneffective.
We have recently designed a novel type of functional nanoparticles with regular icosahedral symmetry, mimicking small, rigid
viral capsids (Fig. 1 (A)) and a diameter of about 17 nm (Fig. 1 (C)) which self-assemble from single polypeptide chains (Fig.
1 (B)). 相似文献
42.
Human C-reactive protein (CRP) is a clinically important classical acute phase protein. Although CRP has been reported to
bind with many nucleated cells, the direct binding of CRP to erythrocytes in diseases remains largely unexplored. The main
focus of the present study was to investigate the binding of disease-specific CRP to erythrocytes of same patients. Distinct
molecular variant of disease-specific CRP was affinity purified from sera of malaria patients (CRPMal). This CRP showed strong binding with malaria erythrocytes (RBCMal) as confirmed by flow cytometric analysis (FACS), enzyme-linked immunosorbent assays (ELISA), and radio binding assays. Calcium
and phosphoryl choline (PC) were found to be essential for this interaction. A 2.3-fold increased binding of induced CRP to
RBCMal as compared to normal erythrocytes (RBCN) confirmed disease-specificity. Preincubation of RBCMal with unconjugated CRP showed 3–5 fold inhibition. The association constant of CRP and RBCMal was 4.7 × 106 cpm/μg with the corresponding number of receptors/cell being 4.3 × 105. The effector function of CRPMal has been demonstrated by its potency to activate the complement pathway. An optimal dose of 10 μg/ml of CRP induced three-fold
higher hemolysis of patient erythrocytes as compared to RBCN. These studies provide direct evidence for an important phagocytic functional interaction of this acute-phase protein by
triggering the CRP-complement pathway after the binding of CRPMal with RBCMal. Hemolysis as triggered by this pathway may be one of the causative factors of anemia, a common clinical manifestation of
this disease. 相似文献
43.