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Open AccessArticle

Encapsulating TGF-β1 Inhibitory Peptides P17 and P144 as a Promising Strategy to Facilitate Their Dissolution and to Improve Their Functionalization

Nanomedicine Department, Institute of Nanoscience and Nanotechnology, Kafrelsheikh University, Kafrelsheikh 33516, Egypt
Bellvitge Biomedical Research Institute (IDIBELL), University of Barcelona (UB) and CIBEREHD, Gran Via de l’Hospitalet, 199, Hospitalet de Llobregat, 08908 Barcelona, Spain
CNR NANOTEC-Istituto di Nanotecnologia, Via Monteroni, 73100 Lecce, Italy
Authors to whom correspondence should be addressed.
Pharmaceutics 2020, 12(5), 421;
Received: 24 March 2020 / Revised: 28 April 2020 / Accepted: 29 April 2020 / Published: 2 May 2020
(This article belongs to the Special Issue Nano-Micro Encapsulation of Drugs)
Transforming growth factor-beta (TGFβ1) is considered as a master regulator for many intracellular signaling pathways, including proliferation, differentiation and death, both in health and disease. It further represents an oncogenic factor in advanced tumors allowing cancer cells to be more invasive and prone to move into the metastatic process. This finding has received great attention for discovering new therapeutic molecules against the TGFβ1 pathway. Among many TGFβ1 inhibitors, peptides (P17 and P144) were designed to block the TGFβ1 pathway. However, their therapeutic applications have limited use, due to lack of selection for their targets and their possible recognition by the immune system and further due to their potential cytotoxicity on healthy cells. Besides that, P144 is a highly hydrophobic molecule with less dissolution even in organic solution. Here, we aimed to overcome the dissolution of P144, as well as design nano-delivery strategies to protect normal cells, to increase cellular penetration and to raise the targeted therapy of both P17 and P144. Peptides were encapsulated in moieties of polymer hybrid protein. Their assembly was investigated by TEM, microplate spectrum analysis and fluorescence microscopy. SMAD phosphorylation was analyzed by Western blot as a hallmark of their biological efficiency. The results showed that the encapsulation of P17 and P144 might improve their potential therapeutic applications. View Full-Text
Keywords: transforming growth factors; proliferation; polymer hybrid protein transforming growth factors; proliferation; polymer hybrid protein
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Hanafy, N.A.N.; Fabregat, I.; Leporatti, S.; El Kemary, M. Encapsulating TGF-β1 Inhibitory Peptides P17 and P144 as a Promising Strategy to Facilitate Their Dissolution and to Improve Their Functionalization. Pharmaceutics 2020, 12, 421.

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