Profiling Of Volatiles In Tissues Of Salacia Reticulata Wight. With Anti-Diabetic Potential Using GC-MS And Molecular Docking

TL;DR

This study identifies volatile compounds in Salacia reticulata tissues using GC-MS, evaluates their drug-like properties, and assesses their potential as anti-diabetic agents through molecular docking, offering promising natural alternatives to conventional drugs.

Contribution

It provides a comprehensive profiling of volatile compounds in Salacia reticulata and evaluates their anti-diabetic potential via molecular docking, highlighting novel bioactive candidates.

Findings

Identification of key volatile compounds with drug-like properties

Compounds CID-240051 and CID-533471 show high binding affinity to target enzyme

Potential natural inhibitors for type 2 diabetes treatment

Abstract

Type 2 diabetes mellitus is a global pandemic, it is a chronic, progressive and an incompletely understood metabolic condition. The disease is characterized by higher levels of sugar in blood caused either due to insufficient production of insulin or because of insulin resistance. Major drugs used for the treatment of the condition are fraught with side effects. Hence, it is becoming an obligation to gaze at alternative agents showing marginal adverse effects. An important source of such agents are the medicinal plants. Several plants have been positively identified to show anti-diabetic effects. The species Salacia reticulata Wight., belonging to the family Celastraceae which is found in the forests of Southern India is one such promising plant to tackle type 2 diabetics. In this study, numerous volatile compounds were identified from various tissues through GC-MS analysis. Among these the compounds possessed suitable ADMET properties, and high binding affinities were compared with two approved {\alpha}-glucosidase inhibitors, Acarbose and Miglitol. The analysis indicated that the compounds with PubChem IDs, CID-240051 and CID-533471 exhibited potential as inhibitors of Human Maltase-Glucoamylase enzyme.