ABSTRACT
Arrowhead (Sagittaria trifolia var. sinensis) is a source of starch worldwide, but arrowhead starch has been rarely studied. In this work, starch was separated from arrowhead corm. The morphology and physicochemical properties of starch were then investigated and compared among 3 different arrowhead varieties (Purple-corm, Hongta, and Japanese). Results showed that starches from the 3 varieties similarly featured an oval shape containing a visible polarization cross, a CA -type crystalline structure, and an ordered structure in the external granule region. However, starch content, granule size, crystal characteristics, and pasting properties differed among the 3 varieties. Japanese arrowhead exhibited the highest starch content and degree of ordered structure in the external granule region, as well as onset, peak, and final gelatinization temperature. Purple-corm arrowhead starch demonstrated the highest amylose content and relative degree of crystallinity, smallest granule size, and lowest swelling power and solubility. Purple-corm arrowhead starch also showed the highest gelatinization enthalpy, as well as peak, trough, final, and setback viscosities. This starch further presented the lowest breakdown viscosity and degree of hydrolysis by HCl and porcine pancreatic α-amylase. These findings can provide useful references for arrowhead variety selection in food and nonfood industries.
Subject(s)
Plant Tubers/chemistry , Sagittaria/chemistry , Starch/chemistry , Amylose/analysis , Animals , Hydrolysis , Molecular Structure , Pancreatic alpha-Amylases/metabolism , Solubility , Species Specificity , Swine , Temperature , Thermodynamics , ViscosityABSTRACT
The thyroid hormones, triiodothyronine and thyroxine, play important roles in cognitive function during the mammalian lifespan. However, thyroid hormones have not yet been used as a therapeutic agent for normal age-related cognitive deficits. In this study, CD-1 mice (aged 24 months) were intraperitoneally injected with levothyroxine (L-T4; 1.6 µg/kg per day) for 3 consecutive months. Our findings revealed a significant improvement in hippocampal cytoskeletal rearrangement of actin and an increase in serum hormone levels of L-T4-treated aged mice. Furthermore, the survival rate of these mice was dramatically increased from 60% to 93.3%. The Morris water maze task indicated that L-T4 restored impaired spatial memory in aged mice. Furthermore, level of choline acetyltransferase, acetylcholine, and superoxide dismutase were increased in these mice, thus suggesting that a possible mechanism by which L-T4 reversed cognitive impairment was caused by increased activity of these markers. Overall, supplement of low-dosage L-T4 may be a potential therapeutic strategy for normal age-related cognitive deficits.
ABSTRACT
PURPOSE: Delivery of therapeutic proteins across the blood-brain barrier (BBB) is severely limited by their size and biochemical properties. Here we showed that a 39-amino acid peptide derived from the rabies virus glycoprotein (RDP) was exploited as an efficient protein carrier for brain-targeting delivery. METHODS: Three proteins with different molecular weight and pI, ß-galactosidase (ß-Gal), luciferase (Luc) and brain-derived neurotrophic factor (BDNF), were fused to RDP and intravenously injected into the mice respectively. The slices of different tissues with X-Gal staining were used to examine whether RDP could deliver ß-Gal targeted into the CNS. The time-course relationship of RDP-Luc was studied to confirm the transport efficiency of RDP. The neuroprotective function of RDP-BDNF was examined in mouse experimental stroke to explore the pharmacological effect of RDP fusion protein. RESULTS: The results showed that the fusion proteins rapidly and specific entered the nerve cells in 15 min, and the t(1/2) was about 1 hr. Furthermore, RDP-BDNF fusion protein showed the neuroprotective properties in mouse experimental stroke including reduction of stroke volume and neural deficit. CONCLUSIONS: RDP provides an effective approach for the targeted delivery of biological active proteins into the central nervous system.
Subject(s)
Blood-Brain Barrier/metabolism , Brain-Derived Neurotrophic Factor/pharmacokinetics , Drug Carriers , Glycoproteins/pharmacokinetics , Neuroprotective Agents/pharmacokinetics , Peptide Fragments/pharmacokinetics , Rabies virus/metabolism , Viral Proteins/pharmacokinetics , Animals , Brain-Derived Neurotrophic Factor/administration & dosage , Brain-Derived Neurotrophic Factor/chemistry , Capillary Permeability , Chemistry, Pharmaceutical , Disease Models, Animal , Drug Compounding , Glycoproteins/administration & dosage , Glycoproteins/chemistry , Half-Life , Humans , Infarction, Middle Cerebral Artery/drug therapy , Infarction, Middle Cerebral Artery/metabolism , Infarction, Middle Cerebral Artery/pathology , Injections, Intravenous , Luciferases/administration & dosage , Luciferases/chemistry , Luciferases/pharmacokinetics , Male , Mice , Neuroprotective Agents/administration & dosage , Neuroprotective Agents/chemistry , Peptide Fragments/administration & dosage , Peptide Fragments/chemistry , Recombinant Fusion Proteins/administration & dosage , Recombinant Fusion Proteins/chemistry , Recombinant Fusion Proteins/pharmacokinetics , Technology, Pharmaceutical/methods , Tissue Distribution , Viral Proteins/administration & dosage , Viral Proteins/chemistry , beta-Galactosidase/administration & dosage , beta-Galactosidase/chemistry , beta-Galactosidase/pharmacokineticsABSTRACT
Targeted delivery of proteins into the hippocampus has not yet been achieved. Here, we show that systemic administration of the ß-galactosidase, fused to a 43-amino-acid peptide derived from rabies virus glycoprotein (RVG), results in targeted delivery of the fusion protein into the hippocampal neurons. This approach may enable the development of protein therapy for neurodegenerative diseases, such as Alzheimer's disease. This result may open new possibilities in using neurotropic virus glycoprotein-derived peptides for targeted delivery of therapeutic molecules into local brain regions.
