Guava is considered as poor man's apple rich in phytochemicals with medicinal value and hence it is highly consumed. Gas chromatography-mass spectroscopy (GC-MS) analysis of guava leaf extract revealed the presence of various bioactive compounds with antimicrobial, antioxidant, anticancer, and antitumor properties. Hence, it is used in tooth paste formulations along with other ingredients such as Acacia arabica gum powder, stevia herb powder, sea salt, extra virgin coconut oil, peppermint oil in the present study. Three formulations F1, F2 and F3 have been made by varying the concentration of these ingredients and the prepared formulations were studied for their antimicrobial activity and physico-chemical parameters such as pH, abrasiveness, foaming activity, spreading and cleaning ability. Among these, F3 showed significant antioxidant and antimicrobial properties, minimal cytotoxicity, maximum spreadability and very high cleaning ability. This study surmises that the herbal toothpaste formulation is greener, rich in medicinal values and imparts oral hygiene.
Yip1 domain family (YIPF) proteins are multi-span, transmembrane proteins mainly localized in the Golgi apparatus. YIPF proteins have been found in virtually all eukaryotes, suggesting that they have essential function(s). Saccharomyces cerevisiae contains four YIPFs: Yip1p, Yif1p, Yip4p, and Yip5p. Early analyses in S. cerevisiae indicated that Yip1p and Yif1p bind to each other and play a role in budding of transport vesicles and/or fusion of vesicles to target membranes. However, the molecular basis of their functions remains unclear. Analysis of YIPF proteins in mammalian cells has yielded significant clues about the function of these proteins. Human cells have nine family members that appear to have overlapping functions. These YIPF proteins are divided into two sub-families: YIPFα/Yip1p and YIPFβ/Yif1p. A YIPFα molecule forms a complex with a specific partner YIPFβ molecule. In the most broadly hypothesized scenario, a basic tetramer complex is formed from two molecules of each partner YIPF protein, and this tetramer forms a higher order oligomer. Three distinct YIPF protein complexes are formed from pairs of YIPFα and YIPFβ proteins. These are differently localized in either the early, middle, or late compartments of the Golgi apparatus and are recycled between adjacent compartments. Because a YIPF protein is predicted to have five transmembrane segments, a YIPF tetramer complex is predicted to have 20 transmembrane segments. This high number of transmembrane segments suggests that YIPF complexes function as channels, transporters, or transmembrane receptors. Here, the evidence from functional studies of YIPF proteins obtained during the last two decades is summarized and discussed.
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