| dc.contributor.advisor | Kurniatin, Popi Asri | |
| dc.contributor.advisor | Ambarsari, Laksmi | |
| dc.contributor.author | Qonita, Armida Bahy | |
| dc.date.accessioned | 2022-07-02T00:27:28Z | |
| dc.date.available | 2022-07-02T00:27:28Z | |
| dc.date.issued | 2022 | |
| dc.identifier.uri | http://repository.ipb.ac.id/handle/123456789/112242 | |
| dc.description.abstract | Matrix Metalloproteinase-1 (MMP-1) adalah enzim yang berperan menginduksi photoaging dan photocarcinogenesis melalui kolagenolisis pada kulit akibat radiasi UV yang sangat rentan terjadi pada masyarakat Indonesia. Peptida sintetis sebagai bahan kosmetik inhibitor MMP-1 lebih menguntungkan dari segi bioavailabilitas dan toksisitas. Penelitian ini bertujuan mendesain tripeptida sintetis inhibitor MMP-1 berdasarkan struktur kolagen serta penapisan melalui penambatan molekuler di YASARA Structure dan prediksi bioavaibilitas dan toksisitas. Desain tripeptida berdasarkan residu situs pengikatan MMP-1 pada kolagen manusia tipe-I dan III, dilanjutkan dengan penapisan tripeptida dengan residu situs pemotongan kolagen, serta keberadaan residu hidrofobik menghasilkan 636 tripeptida potensial inhibitor MMP-1. Prediksi bioavailabilitas dan toksisitas tripeptida untuk aplikasi topikal terhadap 20 ligan dengan energi pengikatan dan konstanta disosiasi terkecil menunjukkan bahwa 10 ligan memenuhi syarat dengan rentang ΔG -8,229 hingga -7,970 kkal/mol. Ligan alami, ligan pembanding, tripeptida RAT, RTP, RAP, RIR, RLQ, RLR, dan RGT menginhibisi MMP-1 melalui pengikatan dengan Zn katalitik serta residu pengikat substrat, sedangkan RGR, PGR, dan RGQ menginhibisi kolagenase-1 melalui pengikatan dengan residu pengikat substrat dan residu katalitik. | id |
| dc.description.sponsorship | Matrix Metalloproteinase-1 (MMP-1) is an enzyme that plays a role in inducing photoaging and photocarcinogenesis through skin collagenolysis skin due to UV radiation that really vulnerable for Indonesian. Synthetic peptides as cosmetic ingredients are more beneficial in terms of bioavailability and toxicity. This study aims to design a synthetic tripeptide inhibitor MMP-1 based on collagen structure through molecular docking in YASARA Structure with molecular interaction analysis on Ligplot+ and PyMol. Tripeptide design based on MMP -1 binding site residues on human collagen type I and III followed by screening of
tripeptide with collagen cleavage site residues and hydrophobic residues resulted in 636 potential tripeptide inhibitors of MMP-1. Predictions of tripeptide’s bioavailability and toxicity for topical application of 20 ligands with small ΔG and
Kd showed 10 qualified ligands ΔG range -8,229 to -7,970 kcal/mol. Its molecular interaction showed that native ligand, Batimastat, RAT, RTP, RAP, RIR, RLQ, RLR, and RGT inhibit MMP-1 through binding to catalytic Zn and substrate-binding residues, whereas others inhibit collagenase-1 by binding to substrate-binding and catalytic residues. | id |
| dc.language.iso | id | id |
| dc.publisher | IPB University | id |
| dc.title | Potensi Tripeptida sebagai Inhibitor Matrix Metalloproteinase-1 untuk Anti Photoaging dan Photocarcinogenesis secara In Silico | id |
| dc.title.alternative | In Silico Analysis of Potential Tripeptide as Matrix Metalloproteinase-1 Inhibitor for Antiphotoaging and Photocarcinogenesis | id |
| dc.type | Undergraduate Thesis | id |
| dc.subject.keyword | anti-photoaging | id |
| dc.subject.keyword | anti-photocarcinogenesis | id |
| dc.subject.keyword | matrix metalloproteinase-1 | id |
| dc.subject.keyword | molecular docking | id |
| dc.subject.keyword | tripeptide design | id |
