چاپ صفحه |  صفحه نخست سامانه |  نویسندگان |  اطلاعات تفضیلی |  دانلود مقاله | دانشگاه علوم پزشکی تبریز |
| نویسنده | نفر چندم مقاله |
|---|---|
| لیلا رهبرنیا | دوم |
| سمیه نبی زاده | اول |
| عنوان | متن |
|---|---|
| کلمات کلیدی | Antimicrobial peptide, anticancer peptide, melittin, TAT, hybrid peptide |
| خلاصه مقاله | Background: Melittin (GIGAVLKVLTTGLPALISWIKRKRQQ) as a small peptide constituent of bee venom is considered as one of the promising candidates for anticancer therapy. It can target interaction between CD147 and CypA molecule to inhibit the caspase pathway. However, its clinical applicability is limited because of low penetration into cancer cells. TAT is an arginine-rich, cell-penetrating peptide that is widely used to deliver different therapeutic molecules into cells. Materials and methods: For this, PDB, CAMPR3, and APD databases were used to evaluate physicochemical properties and also the selection of amino acid regions with high anti-cancer activity in melittin and Tat peptides. AntiCP server was used to predict novel analogs of melittin with higher anti-cancer property based on SVM score. Cluspro was used to study interaction between peptide and CD147 /CypA complex. Molecular dynamic and Coarse grained simulations were employed to examine the stability of designed peptide as well as the interation between peptide with cancer membrane model. Results: A hybrid peptide was designed with more stability and penetration into cancer cells through fusion between analogs of melittin and TAT. An amino acid region with high anti-cancer activity in Melittin was selected based on the physicochemical properties. Based on the results, a truncated Melittin peptide with 15 amino acids by the GGGS linker was fused to a TAT peptide (nine amino acids) to increase the penetration rate into the cell. A new hybrid peptide analog was designed via replacing the glycine with serine through random point mutation. Based on Clus Pro Docking results, the designed peptide acts as an inhibitory peptide with high binding energy when interacting with CD147 and the CypA proteins. RMSD and RMSF results confirmed the high stability of designed peptide in interaction with CD147. Also, the coarse-grained simulation showed the penetration potential of TM peptide into the DOPS-DOPC model membrane. In conclusion Our findings indicated that the designed multifunctional peptide could be an attractive therapeutic candidate to halter tumor types. |
| نام فایل | تاریخ درج فایل | اندازه فایل | دانلود |
|---|---|---|---|
| Screenshot_20240728-124405_WhatsApp.jpg | 1403/09/04 | 167087 | دانلود |
| anti cancer abstract.jpg | 1403/09/05 | 396728 | دانلود |
| TAT certificate.jpg | 1403/09/05 | 939800 | دانلود |
