KAJIAN IN SILICO PEPTIDA P4-33 TURUNAN ?-GLIADIN SEBAGAI PEPTIDA PENEMBUS SEL (CPP)

• Main Author: Nurul Aeni, Amaliyah
• Format: Final Project
• Language: Indonesia
• Online Access: https://digilib.itb.ac.id/gdl/view/56636
• Institution: Institut Teknologi Bandung

The digested ?-gliadin fragment has been shown to enter into intestinal cells so that it has the potential to become a Cell Pentrating Peptide (CPP). CPP is a short peptide (5-30 amino acids) which has the ability to penetrate into cells. In order for ?-gliadin to be used as CPP, its safety aspects such as toxicity, allergenicity, and antigenicity must be known. The sequence of fragments obtained from gliadin digestion must be known so that they can be further mutated to optimize their capabilities and safety. This study aims to obtain CPP candidates from ?-gliadin with a protein scanning approach. In this study, the optimization of the predicted fragments as CPP from ?-gliadin by means of mutation, namely by substituting the amino acid that make up the sequence. Prediction of potency, toxicity, allergenicity, and antigenicity was done in silico. Potency prediction was done using CellPPD, toxicity prediction using ToxinPred and ToxDL, prediction of antigenicity using ANTIGENpro and ElliPro, and allergenicity using AllergenFP and AllerTOP v.2. The results showed that the peptide with the order FLILALLAIVATTATTAVRVPVPQLQPQHP (P4-33) as a CPP candidate did not have a toxic tetrapeptide motive, was not allergen, and had the highest CPP score of 5.0 (hybrid score) however, P4-33 was antigenic. Mutation of P4-33 was carried out further with the aim of reducing the antigenicity properties but still maintaining the ability to penetrate into cells. F1R, T12R, T15A, V22Q P23A, P27A, and P30R mutations succeeded in reducing antigenicity and increasing the penetration ability of P4- 33 in silico, including reducing detected epitopes, lowering the ANTIGENpro score to 0,18, lowering the ToxDL score to 0,15, and increasing the CPP score to 5,15.