02351nas a2200277   4500008004100000022001400041245010100055210006900156260005700225300001000282490000700292520140100299653001901700653000801719653002201727653002101749653001301770653002201783100002101805700002301826700002101849700002601870700002101896700002501917856013101942       2015                        eng d  a1572-388700aAcid stability of the kinetically stable alkaline serine protease possessing polyproline II fold0 aAcid stability of the kinetically stable alkaline serine proteas  a233 SPRING ST, NEW YORK, NY 10013 USAbSPRINGERcFEB  a60-670 v343 a<p>The kinetically stable alkaline serine protease from Nocardiopsis sp.; NprotI, possessing polyproline II fold (PPII) was characterized for its pH stability using proteolytic assay, fluorescence and Circular Dichroism (CD) spectroscopy, and Differential Scanning Calorimetry (DSC). NprotI was found to be functionally stable when incubated at pH 1.0, even after 24 h, while after incubation at pH 10.0, drastic loss in the activity was observed. The enzyme showed enhanced activity after incubation at pH 1.0 and 3.0, at higher temperature (50-60 A degrees C). NprotI maintained the overall PPII fold in broad pH range as seen using far UV CD spectroscopy. The PPII fold of NprotI incubated at pH 1.0 remained fairly intact up to 70 A degrees C. Based on the isodichroic point and T-m values revealed by secondary structural transitions, different modes of thermal denaturation at pH 1.0, 5.0 and 10.0 were observed. DSC studies of NprotI incubated at acidic pH (pH 1.0-5.0) showed T-m values in the range of 74-76 A degrees C while significant decrease in T-m (63.8 A degrees C) was observed at pH 10.0. NprotI could be chemically denatured at pH 5.0 (stability pH) only with guanidine thiocynate. NprotI can be classified as type III protein among the three acid denatured states. Acid tolerant and thermostable NprotI can serve as a potential candidate for biotechnological applications.</p>10aAcid stability10aDSC10aKinetic stability10aPolyproline fold10aProtease10aThermal unfolding1 aRohamare, Sonali1 aJavdekar, Vaishali1 aDalal, Sayli, A.1 aNareddy, Pavan, Kumar1 aSwamy, Musti, J.1 aGaikwad, Sushama, M.  uhttps://library.ncl.res.in/content/acid-stability-kinetically-stable-alkaline-serine-protease-possessing-polyproline-ii-fold-002021nas a2200145   4500008004100000245012200041210006900163260000800232490000600240520143500246100001701681700002001698700002501718856013201743       2017                        eng d00aAmaranthus caudatus lectin with polyproline II fold: conformational and functional transitions and molecular dynamics0 aAmaranthus caudatus lectin with polyproline II fold conformation  cJUL0 v13 aPolyproline II (PPII) fold, a peculiar structural element was detected in the Amaranthus caudatus seed lectin (ACL) based on far UV circular dichroism spectrum, conformational transitions of the lectin and a distinct isodichroic point in thermal denaturation. It was confirmed by using PolyprOnline database to estimate the percentage of amino acids contributing to PPII fold and showed the values as 13.5% and 13.9% for PROSS and XTLSSTR, respectively. Investigations of the functional and conformational transitions of ACL during thermal, pH and guanidine hydrochloride (GdnHCl) induced denaturation were carried out using biochemical and biophysical techniques and molecular dynamics (MD) simulations approach. The lectin got aggregated at 60 °C with instantaneous structural alterations. The aggregation-prone regions in ACL were predicted using online servers viz. AGGRESCAN, AmylPred, FoldAmyloid and Waltz that were represented by Visual Molecular Dynamics tools. Nine conserved regions were identified by these softwares as being ‘hot-spots’ for aggregation. MD simulation studies of the lectin at 60 °C revealed increase in radius of gyration. The loss of PPII fold in 2.0 M GdnHCl was reversible. The partially unfolded intermediate of ACL with diminished PPII fold formed at pH 1.0 was stable up to 90 °C. The polyproline II fold has been rarely detected in lectins, ACL being the second after the potato lectin.1 aYadav, Priya1 aShahane, Ganesh1 aGaikwad, Sushama, M.  uhttps://library.ncl.res.in/content/amaranthus-caudatus-lectin-polyproline-ii-fold-conformational-and-functional-transitions-and02234nas a2200277   4500008004100000022001400041245011600055210006900171260000800240300001200248490000700260520132600267653001601593653002201609653001401631653001401645653002201659653001201681653001001693653002801703100002801731700001601759700002701775700002501802856012901827       2020                        eng d  a0929-866500aAnticancer activity of lectins from bauhinia purpurea and wisteria floribunda on breast cancer MCF-7 cell lines0 aAnticancer activity of lectins from bauhinia purpurea and wister  cJAN  a870-8770 v273 a<p>Background: Individual and collaborative efforts are being made worldwide in search of effective chemical or natural drugs with less severe side-effects for treatment of cancer. Due to the specificity and selectivity properties of lectins for saccharides, several plant lectins are known to induce cytotoxicity into tumor cells. Objective: To study the antiproliferative activity of two N-acetyl galactosamine specific plant lectins from seeds of Bauhinia purpurea and Wisteria floribunda against MCF-7 Breast cancer cell lines. Methods: MTT, lactate dehydrogenase (LDH) leakage, reactive oxygen species (ROS), and caspase-3 assays and flow cytometry for cell cycle analysis were performed. Results: The agglutinins BPL and WFL; 446 mu gml(-1) (2.2 mu M) and 329 mu gml(-1) (2.8 mu M), respectively caused remarkable concentration-dependent antiproliferative effect on MCF-7. The effect was seen to be a consequence of binding of the lectin to the cell surface and triggering S and G2 phase arrest. Apoptosis induced was found to be associated with LDH leakage, cell cycle arrest and ROS generation. The apoptotic signal was observed to be amplified by activation of caspase-3 resulting in cell death. Conclusion: The study provides a base for detailed investigation and further use of lectins in cancer studies.</p>
10aanti-cancer10aantiproliferative10aApoptosis10acaspase-310acell cycle arrest10aLectins10aMCF-710areactive oxygen species1 aAgrawal, Sanskruthi, B.1 aGupta, Neha1 aBhagyawant, Sameer, S.1 aGaikwad, Sushama, M.  uhttps://library.ncl.res.in/content/anticancer-activity-lectins-bauhinia-purpurea-and-wisteria-floribunda-breast-cancer-mcf-7