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Peptide Based Smart Molecules in Regenerative Medicine
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Peptide Based Smart Molecules in Regenerative Medicine

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Pathology, Diagnostics, and Therapeutics".

Deadline for manuscript submissions: closed (15 June 2021) | Viewed by 9924

Special Issue Editor

Prof. Dr. Yoon Jeong Park

E-Mail Website
Guest Editor
Department of Oral Biochemistry/Dental Regenerative Biotechnology, Seoul National University, Seoul, Korea
Interests: intracellular delivery of protein drugs and genes; Tissue engineering for tissue regeneration

Special Issue Information

Dear Colleagues,

The field of regenerative medicine has gained scientific attention, with some success through milestone discoveries in stem cell biology, tissue engineering, and drug delivery systems, which have been the main driving paradigm shifts in the pharmacotherapy of degenerative, metabolic, inflammatory diseases, and even the oncology field. Smart molecules, including tissue recognizing/reactive peptides, small molecules, proteins, peptide–protein fusion materials, and polymeric drugs, are of paramount interest in regenerative medicine due to their selective mode of action in the course of regeneration. These smart materials are more and more crucial in advanced tissue engineering. Smart molecules by themselves or in combination with polymeric biomaterials for controlled/targeted drug delivery offer a powerful solution to improve therapeutic efficacy. Understanding smart molecule based regeneration, followed by therapeutic efficacy, may be useful for regenerative medicine and pharmaceutical technology.

The aim of this Special Issue on “Peptide-Based Smart Molecules in Regenerative Medicine” will comprise a selection of research papers and reviews contributing to the application of peptides as a signal molecule of tissue regeneration or as a smart drug delivery carrier. Contributions to the Special Issue can be original research or review articles and may cover peptide-based molecule or peptide delivery carriers to direct selective cell signaling, differentiation, tissue regeneration or drug delivery, which are essential for the success of regenerative medicine.

Prof. Dr. Yoon Jeong Park
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. International Journal of Molecular Sciences is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. There is an Article Processing Charge (APC) for publication in this open access journal. For details about the APC please see here. Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • Peptide
  • Smart molecule
  • Peptide carrier
  • Tissue engineering
  • Drug delivery system
  • Regenerative medicine

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Published Papers (3 papers)

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Research

13 pages, 3873 KiB  
Article
Cell-Permeable Oct4 Gene Delivery Enhances Stem Cell-like Properties of Mouse Embryonic Fibroblasts
by Da Hyeon Choi, Kyeong Eun Lee, Jiwon Park, Yoon Jeong Park, Jue-Yeon Lee and Yoon Shin Park
Int. J. Mol. Sci. 2021, 22(17), 9357; https://doi.org/10.3390/ijms22179357 - 28 Aug 2021
Cited by 2 | Viewed by 2498
Abstract
Direct conversion of one cell type into another is a trans-differentiation process. Recent advances in fibroblast research revealed that epithelial cells can give rise to fibroblasts by epithelial-mesenchymal transition. Conversely, fibroblasts can also give rise to epithelia by undergoing a mesenchymal to epithelial [...] Read more.
Direct conversion of one cell type into another is a trans-differentiation process. Recent advances in fibroblast research revealed that epithelial cells can give rise to fibroblasts by epithelial-mesenchymal transition. Conversely, fibroblasts can also give rise to epithelia by undergoing a mesenchymal to epithelial transition. To elicit stem cell-like properties in fibroblasts, the Oct4 transcription factor acts as a master transcriptional regulator for reprogramming somatic cells. Notably, the production of gene complexes with cell-permeable peptides, such as low-molecular-weight protamine (LMWP), was proposed to induce reprogramming without cytotoxicity and genomic mutation. We designed a complex with non-cytotoxic LMWP to prevent the degradation of Oct4 and revealed that the positively charged cell-permeable LMWP helped condense the size of the Oct4-LMWP complexes (1:5 N:P ratio). When the Oct4-LMWP complex was delivered into mouse embryonic fibroblasts (MEFs), stemness-related gene expression increased while fibroblast intrinsic properties decreased. We believe that the Oct4-LMWP complex developed in this study can be used to reprogram terminally differentiated somatic cells or convert them into stem cell-like cells without risk of cell death, improving the stemness level and stability of existing direct conversion techniques. Full article
(This article belongs to the Special Issue Peptide Based Smart Molecules in Regenerative Medicine)
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14 pages, 2406 KiB  
Article
The Prominin-1-Derived Peptide Improves Cardiac Function Following Ischemia
by Avner Adini, Irit Adini, Etty Grad, Yuval Tal, Haim D. Danenberg, Peter M. Kang, Benjamin D. Matthews and Robert J. D’Amato
Int. J. Mol. Sci. 2021, 22(10), 5169; https://doi.org/10.3390/ijms22105169 - 13 May 2021
Cited by 5 | Viewed by 2631
Abstract
Myocardial infarction (MI) remains the leading cause of death in the western world. Despite advancements in interventional revascularization technologies, many patients are not candidates for them due to comorbidities or lack of local resources. Non-invasive approaches to accelerate revascularization within ischemic tissues through [...] Read more.
Myocardial infarction (MI) remains the leading cause of death in the western world. Despite advancements in interventional revascularization technologies, many patients are not candidates for them due to comorbidities or lack of local resources. Non-invasive approaches to accelerate revascularization within ischemic tissues through angiogenesis by providing Vascular Endothelial Growth Factor (VEGF) in protein or gene form has been effective in animal models but not in humans likely due to its short half-life and systemic toxicity. Here, we tested the hypothesis that PR1P, a small VEGF binding peptide that we developed, which stabilizes and upregulates endogenous VEGF, could be used to improve outcome from MI in rodents. To test this hypothesis, we induced MI in mice and rats via left coronary artery ligation and then treated animals with every other day intraperitoneal PR1P or scrambled peptide for 14 days. Hemodynamic monitoring and echocardiography in mice and echocardiography in rats at 14 days showed PR1P significantly improved multiple functional markers of heart function, including stroke volume and cardiac output. Furthermore, molecular biology and histological analyses of tissue samples showed that systemic PR1P targeted, stabilized and upregulated endogenous VEGF within ischemic myocardium. We conclude that PR1P is a potential non-invasive candidate therapeutic for MI. Full article
(This article belongs to the Special Issue Peptide Based Smart Molecules in Regenerative Medicine)
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27 pages, 6398 KiB  
Article
Design and Evaluation of a Polypeptide that Mimics the Integrin Binding Site for EDA Fibronectin to Block Profibrotic Cell Activity
by Lin Zhang, Hongyu Yan, Yifan Tai, Yueming Xue, Yongzhen Wei, Kai Wang, Qiang Zhao, Shufang Wang, Deling Kong and Adam C. Midgley
Int. J. Mol. Sci. 2021, 22(4), 1575; https://doi.org/10.3390/ijms22041575 - 4 Feb 2021
Cited by 10 | Viewed by 4179
Abstract
Fibrosis is characterized by excessive production of disorganized collagen- and fibronectin-rich extracellular matrices (ECMs) and is driven by the persistence of myofibroblasts within tissues. A key protein contributing to myofibroblast differentiation is extra domain A fibronectin (EDA-FN). We sought to target and interfere [...] Read more.
Fibrosis is characterized by excessive production of disorganized collagen- and fibronectin-rich extracellular matrices (ECMs) and is driven by the persistence of myofibroblasts within tissues. A key protein contributing to myofibroblast differentiation is extra domain A fibronectin (EDA-FN). We sought to target and interfere with interactions between EDA-FN and its integrin receptors to effectively inhibit profibrotic activity and myofibroblast formation. Molecular docking was used to assist in the design of a blocking polypeptide (antifibrotic 38-amino-acid polypeptide, AF38Pep) for specific inhibition of EDA-FN associations with the fibroblast-expressed integrins α4β1 and α4β7. Blocking peptides were designed and evaluated in silico before synthesis, confirmation of binding specificity, and evaluation in vitro. We identified the high-affinity EDA-FN C-C′ loop binding cleft within integrins α4β1 and α4β7. The polypeptide with the highest predicted binding affinity, AF38Pep, was synthesized and could achieve specific binding to myofibroblast fibronectin-rich ECM and EDA-FN C-C′ loop peptides. AF38Pep demonstrated potent myofibroblast inhibitory activity at 10 µg/mL and was not cytotoxic. Treatment with AF38Pep prevented integrin α4β1-mediated focal adhesion kinase (FAK) activation and early signaling through extracellular-signal-regulated kinases 1 and 2 (ERK1/2), attenuated the expression of pro-matrix metalloproteinase 9 (MMP9) and pro-MMP2, and inhibited collagen synthesis and deposition. Immunocytochemistry staining revealed an inhibition of α-smooth muscle actin (α-SMA) incorporation into actin stress fibers and attenuated cell contraction. Increases in the expression of mRNA associated with fibrosis and downstream from integrin signaling were inhibited by treatment with AF38Pep. Our study suggested that AF38Pep could successfully interfere with EDA-FN C-C′ loop-specific integrin interactions and could act as an effective inhibitor of fibroblast of myofibroblast differentiation. Full article
(This article belongs to the Special Issue Peptide Based Smart Molecules in Regenerative Medicine)
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