Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0011860 (type 2 diabetes)
 57,723 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Rice bran proteins (RBP) have been demonstrated to harbour biologically active peptides, which can be released by proteases and applied in human health promotion. In this study, the roles of rice bran cysteine protease inhibitors, oryzacystatins, were considered for efficient production of bioactive peptides from RBP. In silico evidence demonstrates that aspartate protease (pepsin at pH>2) and metalloproteinase (thermolysin) have strong prospects for use in simultaneously cleaving the QXVXGX motif of oryzacystatins, which can lead to their inactivation, and in releasing bioactive sequences from the protease inhibitors. The cleaved bioactive peptides are known to possess activities that can be applied in the management of hypertension, oxidative stress, type 2 diabetes mellitus and other aberrant cellular processes. Moreover, several potentially bioactive di- and tripeptides were identified in oryzacystatin peptide pools. This study provides an important consideration and a direction that can lead to efficient release of bioactive peptides from rice bran proteins for functional food applications.
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PMID:Towards rice bran protein utilization: In silico insight on the role of oryzacystatins in biologically-active peptide production. 2625 12

In silico and in vitro parameters were used to assess the potential of pigeon pea (Cajanus cajan) nutrient reservoir proteins as sources of dipeptidyl peptidase (DPP)-4 inhibitors. In silico, 40 pigeon pea proteins evaluated had 46% of amino acids associated with DPP-4 inhibition. After virtual hydrolysis, pepsin had the highest frequency of release and bioactivity of released DPP-4 inhibiting peptides, compared to papain and thermolysin. In vitro, thermolysin released the most active DPP-4 inhibitors. The protein hydrolysates contained similar amino acids but different particle sizes. Thus, the bioactivity patterns are attributable to the different nature and behavior of proteins/peptides under actual and virtual conditions. Using eight physicochemical variables, a random forest model with moderate prediction accuracy was developed for predicting DPP-4 inhibitory activity of papain hydrolysates. The findings demonstrate that proteins from pigeon pea are precursors of DPP-4 inhibitors, with potential use in formulating functional food for managing type 2 diabetes. PRACTICAL APPLICATIONS: The emerging use of in silico simulations to predict bioactivity of peptides can provide a framework to direct further wet lab assessments. This pattern can enhance focusing on factors relevant to the bioactive properties of interest. However, there is still limited evidence to confirm the reliability and accuracy of this tool. This study therefore provides insight into the practical use of in silico simulations to predict bioactivity of food peptides by assessing the factors relevant to the enzymatic release of dipeptidyl peptidase-4 inhibitors from pigeon pea seed storage proteins and validating the findings with wet lab assessment. This work also provides important information that can enhance the utilization of pigeon pea, which is an orphan crop, in developing functional food products for managing type 2 diabetes mellitus in developing countries.
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PMID:Enzymatic release of dipeptidyl peptidase-4 inhibitors (gliptins) from pigeon pea (Cajanus cajan) nutrient reservoir proteins: In silico and in vitro assessments. 3157 95