Nanoparticles Loaded with a Carotenoid-Rich Extract from Cantaloupe Melon Improved Hepatic Retinol Levels in a Diet-Induced Obesity Preclinical Model.

The study evaluated the effect of the carotenoid-rich extract from cantaloupe melon (CE) nanoencapsulated in porcine gelatin (EPG) on hepatic retinol concentration and liver damage scores in Wistar rats with obesity induced by high glycemic index and high glycemic load diet (HGLI diet). For 17 days, animals were fed the HGLI diet. They were divided into three groups and treated for 10 days [HGLI diet + water, HGLI diet + CE (12.5 mg/kg), and HGLI diet + EPG (50 mg/kg)]. The groups were evaluated for dietary intake, retinol, weight variation, hematological parameters, fasting glucose, lipid profile, hepatic retinol concentration, AST/ALT ratio, FIB-4 (Fibrosis-4 Index for Liver Fibrosis), and APRI (AST to Platelet Ratio Index) scores to evaluate the effects on the liver. Animals treated with EPG showed a lower dietary intake (p < 0.05). No significant weight change was detected in the evaluated groups (p > 0.05). The EPG-treated group had significantly higher concentrations (p < 0.05) of hepatic retinol [266 (45) µg/g] than the untreated group [186 (23.8) µg/g] and the one treated with CE [175 (8.08) µg/g]. Liver damage assessment scores did not show significant differences, but the lowest means were observed in the group treated with EPG. The nanoencapsulation of the extract rich in beta-carotene promoted reduced food consumption and increased hepatic retinol without causing significant changes in liver damage scores. Thus, EPG is a candidate for future clinical studies to evaluate the beneficial effects of treating diseases involving vitamin A deficiencies.

Mechanism of the action of bioactive proteins of vegetables in diabetes mellitus type 2: Systematic review protocol.

BACKGROUND: Diabetes mellitus type 2 (DM2) is a chronic disease of significant prevalence causing hyperglycemia and several comorbidities. Evidences highlight the performance of non - protein bioactive compounds found in vegetables in the control of hyperglycemia. This study describes a protocol of a systematic review, which analyzes the action of proteins and bioactive peptides of plants in DM2. METHODS: The Preferred Reporting Items guide this protocol for Systematic Reviews and Meta-Analyzes Protocols (PRISMA-P) was used. The databases that will be used for searching will be PubMed, ScienceDirect, Scopus, Web of Science, EMBASE, and Virtual Health Library, Brazil (VHL). Studies that use bioactive proteins and peptides of vegetal origin in DM2 will be included in the systematic review. The studies will be identified using clinical parameters and the effect on insulin resistance. The characteristics of the studies as control groups, test substance, dosage, intervention time, and the main results will be described. Selection of studies, data extraction, and methodological quality assessment will be performed independently by two experienced reviewers. RESULTS: This protocol will be the basis for a systematic review identifying the mechanism of action of plant proteins and peptides in type 2 diabetes mellitus. CONCLUSION: Systematic reviews from this protocol will provide support for the construction of researches that analyze the effect of plant bioactive proteins and peptides on the control of hyperglycemia and how these molecules act in the control of DM2. PROSPERO REGISTRATION NUMBER: CRD42019110956.

Biochemical characterisation of a Kunitz-type inhibitor from Tamarindus indica L. seeds and its efficacy in reducing plasma leptin in an experimental model of obesity.

A trypsin inhibitor isolated from tamarind seed (TTI) has satietogenic effects in animals, increasing the cholecystokinin (CCK) in eutrophy and reducing leptin in obesity. We purified TTI (pTTI), characterised, and observed its effect upon CCK and leptin in obese Wistar rats. By HPLC, and after amplification of resolution, two protein fractions were observed: Fr1 and Fr2, with average mass of [M + 14H]+ = 19,594,690 Da and [M + 13H]+ = 19,578,266 Da, respectively. The protein fractions showed 54 and 53 amino acid residues with the same sequence. pTTI presented resistance to temperature and pH variations; IC50 was 2.7 × 10-10 mol.L-1 and Ki was 2.9 × 10-11 mol.L-1. The 2-DE revealed spots with isoelectric points between pH 5 and 6, and one near pH 8. pTTI action on leptin decrease was confirmed. We conclude that pTTI is a Kunitz trypsin inhibitor with possible biotechnological health-related application.