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Phytochemicals in fruits and vegetables have achieved immense significance owing to the increasing evidence which signifying their activity for antioxidant and prevention of chronic diseases. The amount of phloretin (88.39 µg mg) and phloridzin (83.03 µg mg) were found to be higher among other phenolics determined using UPLC. DPPH, ABTS, metal chelating and ·OH radical assays were used to evaluate antioxidant activity. pulp portion showed higher antioxidant activity than seed portion. HPLC analysis for free amino acids showed that serine (9.06 µg mg), alanine (8.03 µg mg), tyrosine (10.33 µg mg), and cysteine (76.86 µg mg) were only detected in pulp portion while seed comprised of histidine (3.96 µg mg) only. Seed portion was also determined for their fatty acid composition including palmitic acid (0.89%), ethyl palmitate (0.56%), methyl petroselinate (0.90%) and linolein (3.93%) using GC-MS analysis. HPAEC technique detected fructose and sucrose in a fair amount of 21 and 17.3 mg g in pulp, while 9.4 and 4.24 mg g in seed portion, respectively. The present study suggested that fruit is a rich source of phenolic and other chemical components which can be used in food products and nutraceutical formulations.

A key step in the HIV-infection process is the fusion of the virion membrane with the target cell membrane and the concomitant transfer of the viral RNA. Experimental evidence suggests that the fusion is preceded by considerable elastic softening of the cell membranes due to the insertion of fusion peptide in the membrane. What are the mechanisms underpinning the elastic softening of the membrane upon peptide insertion? A broader question may be posed: insertion of rigid proteins in soft membranes ought to stiffen the membranes not soften them. However, experimental observations perplexingly appear to show that rigid proteins may either soften or harden membranes even though conventional wisdom only suggests stiffening. In this work, we argue that regarding proteins as merely non-specific rigid inclusions is flawed, and each protein has a unique mechanical signature dictated by its specific interfacial coupling to the surrounding membrane. Predicated on this hypothesis, we have carried out atomistic simulations to investigate peptide-membrane interactions. Together with a continuum model, we reconcile contrasting experimental data in the literature including the case of HIV-fusion peptide induced softening. We conclude that the structural rearrangements of the lipids around the inclusions cause the softening or stiffening of the biological membranes.

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