Centre for Cellular and Molecular Biology

About: Centre for Cellular and Molecular Biology is a facility organization based out in Hyderabad, India. It is known for research contribution in the topics: Population & Gene. The organization has 2439 authors who have published 3193 publications receiving 97833 citations.

[10]-gingerol induces apoptosis and inhibits metastatic dissemination of triple negative breast cancer in vivo.

Abstract: There is increasing interest in the use of non-toxic natural products for the treatment of various pathologies, including cancer. In particular, biologically active constituents of the ginger oleoresin (Zingiber officinale Roscoe) have been shown to mediate anti-tumour activity and to contribute to the anti-inflammatory, antioxidant, antimicrobial, and antiemetic properties of ginger. Here we report on the inhibitory properties of [10]-gingerol against metastatic triple negative breast cancer (TNBC) in vitro and in vivo. We show that [10]-gingerol concentration-dependently induces apoptotic death in mouse and human TNBC cell lines in vitro. In addition, [10]-gingerol is well tolerated in vivo, induces a marked increase in caspase-3 activation and inhibits orthotopic tumour growth in a syngeneic mouse model of spontaneous breast cancer metastasis. Importantly, using both spontaneous and experimental metastasis assays, we show for the first time that [10]-gingerol significantly inhibits metastasis to multiple organs including lung, bone and brain. Remarkably, inhibition of brain metastasis was observed even when treatment was initiated after surgical removal of the primary tumour. Taken together, these results indicate that [10]-gingerol may be a safe and useful complementary therapy for the treatment of metastatic breast cancer and warrant further investigation of its efficacy, either alone or in combination with standard systemic therapies, in pre-clinical models of metastatic breast cancer and in patients.

Antimicrobial and hemolytic activities of crabrolin, a 13-residue peptide from the venom of the European hornet, Vespa crabro, and its analogs.

Abstract: The venom of insects like bee, hornet and wasp contain peptides that exhibit potent biological activities. Many of these peptides are composed of 13-26 residues and are thus accessible through chemical synthesis as well as amenable to studies directed toward structure-function correlations. In this report, we describe antibacterial and hemolytic activities of crabrolin: FLPLILRKIVTAL-NH2, a 13-residue peptide present in the venom of the hornet Vespa crabro and related peptides. The analogs were chosen so that the role of proline and positively charged amino acids in modulating biological activities could be evaluated. Our results indicate that, although helical conformation is necessary for hemolytic activity, it is not a prerequisite for antibacterial activity. Appropriately positioned, charged and hydrophobic residues and overall hydrophobicity appear to determine antibacterial activity. The discovery of a large number of host-defense peptides in a variety of species in recent years offers a large repertoire of molecules that can be “engineered” based on biophysical principles to yield molecules with specific activities.

Antibacterial activities and conformations of synthetic alpha-defensin HNP-1 and analogs with one, two and three disulfide bridges.

Abstract: Structure and biological activities of synthetic peptides corresponding to human α-defensin HNP-1, AC 1 YC 2 RIPAC 3 IAGERRYGTC 4 IYQGRLWAFC 5 C 6 with the S-S connectivities: C 1 -C 6 , C 2 -C 4 , C 3 -C 5 , and its variants with one, two and three disulfide bridges were investigated. Oxidation of synthetic, reduced HNP-1 yielded a peptide with S-S connectivities C 1 -C 3 , C 2 -C 4 and C 5 -C 6 , and not with the S-S linkages as in naturally occurring HNP-1. Selective protection of cysteine sulfhydryls was necessary for the formation of S-S bridges as in native HNP-1. Likewise, oxidation of peptide encompassing the segment from C 2 to C 5 , resulted in the S-S linkages C 2 -C 3 and C 4 -C 5 instead of the expected linkage C 2 -C 4 and C 3 -C 5 . Antibacterial activities were observed for all peptides, irrespective of how the S-S bridges were linked. Linear peptides without S-S bridges were inactive. Circular dichroism (CD) spectra suggest that peptides constrained by one and two S-S bridges do not form rigid β-sheet structures in an aqueous environment. The spectrum of HNP-1 in an aqueous environment suggests the presence of a β-hairpin conformation. In the presence of lipid vesicles, the S-S constrained peptides tend to adopt a β-structure. Although the S-S connectivities observed in HNP-1 may be necessary for other physiological activities, such as chemotaxis, they are clearly not essential for antibacterial activity.

Two Dictyostelium orthologs of the prokaryotic cell division protein FtsZ localize to mitochondria and are required for the maintenance of normal mitochondrial morphology.

Abstract: In bacteria, the protein FtsZ is the principal component of a ring that constricts the cell at division. Though all mitochondria probably arose through a single, ancient bacterial endosymbiosis, the mitochondria of only certain protists appear to have retained FtsZ, and the protein is absent from the mitochondria of fungi, animals, and higher plants. We have investigated the role that FtsZ plays in mitochondrial division in the genetically tractable protist Dictyostelium discoideum, which has two nuclearly encoded FtsZs, FszA and FszB, that are targeted to the inside of mitochondria. In most wild-type amoebae, the mitochondria are spherical or rod-shaped, but in fsz-null mutants they become elongated into tubules, indicating that a decrease in mitochondrial division has occurred. In support of this role in organelle division, antibodies to FszA and FszA-green fluorescent protein (GFP) show belts and puncta at multiple places along the mitochondria, which may define future or recent sites of division. FszB-GFP, in contrast, locates to an electron-dense, submitochondrial body usually located at one end of the organelle, but how it functions during division is unclear. This is the first demonstration of two differentially localized FtsZs within the one organelle, and it points to a divergence in the roles of these two proteins.

Copper Oxide Nanoparticles Supported on Graphene Oxide‐ Catalyzed S‐Arylation: An Efficient and Ligand‐Free Synthesis of Aryl Sulfides

Abstract: Copper oxide nanoparticles that are sup- ported on graphene oxide as a catalytic system have been utilized for ligand-free and solvent-free CS cross-coupling reactions with weak bases such as tri- A Symmetrical/unsymmetrical aryl sulfides have been synthesized by the coupling of different aryl halides with aromatic as well as aliphatic sul- fides. Surprisingly, aryl chlorides also well reacted with different types of sulfides in the presence of di- methyl sulfoxide and cesium carbonate. Besides, this catalytic system is suitable for the synthesis of phe- nothiazines via cascade CS and CN cross-coupling of ortho-dihalides and ortho-aminobenzothiazoles. In addition, this alternative approach is extremely useful for the synthesis of a variety of symmetrical diaryl sulfides by using thiourea as a sulfur source that is devoid of the foul smell of thiols. Indeed, the calculated E-factor value of our present protocol is 2.52. Furthermore, this protocol is particularly attrac- tive as an environmentally benign and practical method for the synthesis of different aryl sulfides. Moreover, the heterogeneous catalytic system de- scribed in this process represents not only a greener approach but retains its significant activity for up to six catalytic cycles.