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Multi-Functional Collagen-Based Biomaterials for Biomedical Applications

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A special issue of Polymers (ISSN 2073-4360). This special issue belongs to the section "Biobased and Biodegradable Polymers".

Deadline for manuscript submissions: closed (25 February 2023) | Viewed by 52858

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Special Issue Editors

Dr. Nunzia Gallo

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Department of Engineering for Innovation, University of Salento, Via per Monteroni, 73100 Lecce, Italy
Interests: regenerative medicine; medical devices; biomaterials; collagen; scaffolds; drug delivery systems
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Dr. Marta Madaghiele

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Department of Engineering for Innovation, University of Salento, Via per Monteroni, 73100 Lecce, Italy
Interests: polymeric devices for biomedical applications, including scaffolds for regenerative medicine, micro- and nano-particles for controlled drug delivery, wound dressings, and perm-selective barriers for cell encapsulation
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Dr. Alessandra Quarta

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Institute of Nanotechnology, CNR NANOTEC, Campus ECOTEKNE, Via Monteroni, 73100 Lecce, Italy
Interests: nano- and biomaterials; nanoformulations; 3D cell cancer models
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Dr. Amilcare Barca

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Department of Biological and Environmental Sciences and Technologies (DeBEST), Università del Salento, Via per Monteroni c/o Ecotekne, 73100 Lecce, Italy
Interests: cell physiology; comparative and applied physiology; cellular homeostasis; transmembrane transport processes/systems; solute carriers (SLC); epithelial physiology; epithelial cell models; oligopeptides; immunity and inflammation; animal models; zebrafish; cytotoxicity; cell–material interactions; biomaterials; tissue engineering; tissue regeneration
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Polymeric biomaterials are an essential tool in the biomedical field. Their high biocompatibility and ability to provide adequate regenerative support are fundamental for the development of new successful approaches for different therapeutic purposes. In particular, biomaterials derived from living organisms exhibited not only structural roles but also several non-structural functions implicated in cellular growth, migration, and differentiation. For example, type I collagen—an ubiquitarian structural protein present in the mammalian body—plays a dominant role in maintaining the biological and structural integrity of various tissues. In recent years, with the ultimate goal of developing multi-functional collagen-based devices able to better promote the functional recovery of damaged tissues, there have been numerous studies focused on the development of novel techniques and methods for the development and characterization of innovative and advanced high-performance formulations. The ability to control, modify, and tune the performance of collagen-based biomaterials by optimizing scaffolds architecture—besides modifying their chemistry, blending with other materials/therapeutics, or by developing stimuli-responsive formulations—is extremely important information to acquire when specific multi-functionalities are sought. The present Special Issue welcomes contributions in the form of original articles, clinical studies, or review articles, on the broad topic of multi-functional collagen-based biomaterials for biomedical applications, with a focus on any aspect regarding developmental methods (including novel production, processing, and modification of innovative strategies) and a particular attention to the function enhancement of collagen-based formulations. Articles in interdisciplinary areas where the pairing of multiple approaches plays a significant role in the development of multi-functional devices are more than welcome.

Dr. Nunzia Gallo
Dr. Marta Madaghiele
Dr. Alessandra Quarta
Dr. Amilcare Barca
Guest Editors

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Keywords

biomaterials
collagen
tissue engineering
regenerative medicine
scaffold
crosslinking
medical devices
biomedical
biocompatibility

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Published Papers (12 papers)

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Research

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15 pages, 2596 KiB

Open AccessArticle

RETRACTED: The Dosidicus gigas Collagen for Scaffold Preparation and Cell Cultivation: Mechanical and Physicochemical Properties, Morphology, Composition and Cell Viability

by Veronika Anohova, Lyudmila Asyakina, Olga Babich, Olga Dikaya, Aleksandr Goikhman, Ksenia Maksimova, Margarita Grechkina, Maxim Korobenkov, Diana Burkova, Aleksandr Barannikov, Anton Narikovich, Evgeny Chupakhin, Anatoly Snigirev and Sergey Antipov

Polymers 2023, 15(5), 1220; https://doi.org/10.3390/polym15051220 - 28 Feb 2023

Cited by 2 | Viewed by 3400 | Retraction

Abstract

Directed formation of the structure of the culture of living cells is the most important task of tissue engineering. New materials for 3D scaffolds of living tissue are critical for the mass adoption of regenerative medicine protocols. In this manuscript, we demonstrate the results of the molecular structure study of collagen from Dosidicus gigas and reveal the possibility of obtaining a thin membrane material. The collagen membrane is characterized by high flexibility and plasticity as well as mechanical strength. The technology of obtaining collagen scaffolds, as well as the results of studies of its mechanical properties, surface morphology, protein composition, and the process of cell proliferation on its surface, are shown in the given manuscript. The investigation of living tissue culture grown on the surface of a collagen scaffold by X-ray tomography on a synchrotron source made it possible to remodel the structure of the extracellular matrix. It was found that the scaffolds obtained from squid collagen are characterized by a high degree of fibril ordering and high surface roughness and provide efficient directed growth of the cell culture. The resulting material provides the formation of the extracellular matrix and is characterized by a short time to living tissue sorption. Full article

(This article belongs to the Special Issue Multi-Functional Collagen-Based Biomaterials for Biomedical Applications)

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9 pages, 986 KiB

Open AccessCommunication

pH-Dependent Release of Vancomycin from Modularly Assembled Collagen Laminates

by Michelle Fiona Kilb, Ulrike Ritz, Daniela Nickel and Katja Schmitz

Polymers 2022, 14(23), 5227; https://doi.org/10.3390/polym14235227 - 1 Dec 2022

Cited by 1 | Viewed by 1684

Abstract

To prevent surgical site infections, antibiotics can be released from carriers made of biomaterials, such as collagen, that support the healing process and are slowly degraded in the body. In our labs we have developed collagen laminates that can be easily assembled and bonded on-site, according to medical needs. As shown previously, the asymmetric assembly leads to different release rates at the major faces of the laminate. Since the pH changes during the wound healing and infection, we further examined the effect of an acidic and alkaline pH, in comparison to pH 7.4 on the release of vancomycin from different collagen samples. For this purpose, we used an additively manufactured sample holder and quantified the release by HPLC. Our results show that the pH value does not have any influence on the total amount of released vancomycin (atelocollagen sponge pH 5.5: 71 ± 2%, pH 7.4: 68 ± 8%, pH 8.5: 74 ± 3%, bilayer laminate pH 5.5: 61 ± 6%, pH 7.4: 69 ± 4% and pH 8.5: 67 ± 3%) but on the time for half-maximal release. At an acidic pH of 5.5, the swelling of the atelocollagen sponge is largely increased, leading to a 2–3 h retarded release, compared to the physiological pH. No changes in swelling were observed at the basic pH and the compound release was 1–2 h delayed. These effects need to be considered when choosing the materials for the laminate assembly. Full article

(This article belongs to the Special Issue Multi-Functional Collagen-Based Biomaterials for Biomedical Applications)

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23 pages, 5130 KiB

Open AccessArticle

Tailored Polyelectrolyte Multilayer Systems by Variation of Polyelectrolyte Composition and EDC/NHS Cross-Linking: Controlled Drug Release vs. Drug Reservoir Capabilities and Cellular Response for Improved Osseointegration

by Johanna Ludolph, Holger Rothe, Uwe Schirmer, Katharina Möbus, Christina Behrens, Henning Schliephake and Klaus Liefeith

Polymers 2022, 14(20), 4315; https://doi.org/10.3390/polym14204315 - 14 Oct 2022

Cited by 3 | Viewed by 2130

Abstract

Polyelectrolyte multilayers (PEM) are versatile tools used to investigate fundamental interactions between material-related parameters and the resulting performance in stem cell differentiation, respectively, in bone tissue engineering. In the present study, we investigate the suitability of PEMs with a varying collagen content for use as drug carriers for the human bone morphogenetic protein 2 (rhBMP-2). We use three different PEM systems consisting either of the positively charged poly-L-lysine or the glycoprotein collagen type I and the negatively charged glycosaminoglycan heparin. For a specific modification of the loading capacity and the release kinetics, the PEMs were stepwise cross-linked before loading with cytokine. We demonstrate the possibility of immobilizing significant amounts of rhBMP-2 in all multilayer systems and to specifically tune its release via cross-linking. Furthermore, we prove that the drug release of rhBMP-2 plays only a minor role in the differentiation of osteoprogenitor cells. We find a significantly higher influence of the immobilized rhBMP-2 within the collagen-rich coatings that obviously represent an excellent mimicry of the native extracellular matrix. The cytokine immobilized in its bioactive form was able to achieve an increase in orders of magnitude both in the early stages of differentiation and in late calcification compared to the unloaded layers. Full article

(This article belongs to the Special Issue Multi-Functional Collagen-Based Biomaterials for Biomedical Applications)

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15 pages, 3126 KiB

Open AccessArticle

Corneal Stroma Regeneration with Collagen-Based Hydrogel as an Artificial Stroma Equivalent: A Comprehensive In Vivo Study

by Egor Olegovich Osidak, Andrey Yurevich Andreev, Sergey Eduardovich Avetisov, Grigory Victorovich Voronin, Zoya Vasilievna Surnina, Anna Vladimirovna Zhuravleva, Timofei Evgenievich Grigoriev, Sergey Vladimirovich Krasheninnikov, Kirill Konstantinovich Sukhinich, Oleg Vadimovich Zayratyants and Sergey Petrovich Domogatsky

Polymers 2022, 14(19), 4017; https://doi.org/10.3390/polym14194017 - 26 Sep 2022

Cited by 6 | Viewed by 2869

Abstract

Restoring the anatomical and functional characteristics of the cornea using various biomaterials is especially relevant in the context of a global shortage of donor tissue. Such biomaterials must be biocompatible, strong, and transparent. Here, we report a Viscoll collagen membrane with mechanical and optical properties suitable for replacing damaged stromal tissue. After removing a portion of the stroma, a Viscoll collagen membrane was implanted into the corneas of rabbits. After 6 months, the active migration of host cells into Viscoll collagen membranes was noted, with the preservation of corneal transparency in all experimental animals. Effective integration of the Viscoll collagen membrane with corneal tissue promoted nerve regeneration in vivo, as confirmed by in vivo confocal microscopy. We also demonstrated the safety and efficacy of the Viscoll collagen membrane for corneal stroma regeneration. Thus, in combination with the proposed packaging format that provides long-term storage of up to 10 months, this material has great potential for replacing and regenerating damaged stromal tissues. Full article

(This article belongs to the Special Issue Multi-Functional Collagen-Based Biomaterials for Biomedical Applications)

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17 pages, 3129 KiB

Open AccessArticle

Electrospun Collagen Scaffold Bio-Functionalized with Recombinant ICOS-Fc: An Advanced Approach to Promote Bone Remodelling

by Priscila Melo, Giorgia Montalbano, Elena Boggio, Casimiro Luca Gigliotti, Chiara Dianzani, Umberto Dianzani, Chiara Vitale-Brovarone and Sonia Fiorilli

Polymers 2022, 14(18), 3780; https://doi.org/10.3390/polym14183780 - 9 Sep 2022

Cited by 5 | Viewed by 2416

Abstract

The treatment of osteoporotic fractures is a severe clinical issue, especially in cases where low support is provided, e.g., pelvis. New treatments aim to stimulate bone formation in compromised scenarios by using multifunctional biomaterials combined with biofabrication techniques to produce 3D structures (scaffolds) that can support bone formation. Bone’s extracellular matrix (ECM) is mainly composed of type I collagen, making this material highly desirable in bone tissue engineering applications, and its bioactivity can be improved by incorporating specific biomolecules. In this work, type I collagen membranes were produced by electrospinning showing a fibre diameter below 200 nm. An optimized one-step strategy allowed to simultaneously crosslink the electrospun membranes and bind ICOS-Fc, a biomolecule able to reversibly inhibit osteoclast activity. The post-treatment did not alter the ECM-like nanostructure of the meshes and the physicochemical properties of collagen. UV-Vis and TGA analyses confirmed both crosslinking and grafting of ICOS-Fc onto the collagen fibres. The preservation of the biological activity of grafted ICOS-Fc was evidenced by the ability to affect the migratory activity of ICOSL-positive cells. The combination of ICOS-Fc with electrospun collagen represents a promising strategy to design multifunctional devices able to boost bone regeneration in osteoporotic fractures. Full article

(This article belongs to the Special Issue Multi-Functional Collagen-Based Biomaterials for Biomedical Applications)

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16 pages, 4050 KiB

Open AccessArticle

Identification and Characterization of Fibronectin-Binding Peptides in Gelatin

by Yuying Liu, Jianping Gao, Lin Liu, Jiyao Kang, Xi Luo, Yingjun Kong and Guifeng Zhang

Polymers 2022, 14(18), 3757; https://doi.org/10.3390/polym14183757 - 8 Sep 2022

Cited by 1 | Viewed by 2122

Abstract

Collagen and fibronectin (FN) are important components in the extracellular matrix (ECM). Collagen-FN binding belongs to protein-protein interaction and plays a key role in regulating cell behaviors. In this study, FN-binding peptides were isolated from gelatin (degraded collagen) using affinity chromatography, and the amino acid sequences were determined using HPLC-MS. The results indicated that all FN-binding peptides contained GPAG or GPPG. Matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) and dual-polarization interferometry (DPI) were used to analyze the effects of hydroxylation polypeptide on FN binding activity. DPI analysis indicated that peptides with molecular weight (MW) between 2 kDa and 30 kDa showed higher FN-binding activity, indicating MW range played an important role in the interaction between FN and peptides. Finally, two peptides with similar sequences except for hydroxylation of prolines were synthesized. The FN-binding properties of the synthesized peptides were determined by MALDI-TOF MS. For peptide, GAPGADGP*AGAPGTP*GPQGIAGQR, hydroxylation of P8 and P15 is necessary for FN-binding. For peptide, GPPGPMGPPGLAGPPGESGR, the FN-binding process is independent of proline hydroxylation. Thus, FN-binding properties are proline-hydroxylation dependent. Full article

(This article belongs to the Special Issue Multi-Functional Collagen-Based Biomaterials for Biomedical Applications)

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15 pages, 7940 KiB

Open AccessArticle

Customizable Collagen Vitrigel Membranes and Preliminary Results in Corneal Engineering

by María Dolores Montalvo-Parra, Wendy Ortega-Lara, Denise Loya-García, Andrés Bustamante-Arias, Guillermo-Isaac Guerrero-Ramírez, Cesar E. Calzada-Rodríguez, Guiomar Farid Torres-Guerrero, Betsabé Hernández-Sedas, Italia Tatnaí Cárdenas-Rodríguez, Sergio E. Guevara-Quintanilla, Marcelo Salán-Gomez, Miguel Ángel Hernández-Delgado, Salvador Garza-González, Mayra G. Gamboa-Quintanilla, Luis Guillermo Villagómez-Valdez, Judith Zavala and Jorge E. Valdez-García

Polymers 2022, 14(17), 3556; https://doi.org/10.3390/polym14173556 - 29 Aug 2022

Cited by 3 | Viewed by 2986

Abstract

Corneal opacities are a leading cause of visual impairment that affect 4.2 million people annually. The current treatment is corneal transplantation, which is limited by tissue donor shortages. Corneal engineering aims to develop membranes that function as scaffolds in corneal cell transplantation. Here, we describe a method for producing transplantable corneal constructs based on a collagen vitrigel (CVM) membrane and corneal endothelial cells (CECs). The CVMs were produced using increasing volumes of collagen type I: 1X (2.8 μL/mm²), 2X, and 3X. The vitrification process was performed at 40% relative humidity (RH) and 40 °C using a matryoshka-like system consisting of a shaking-oven harboring a desiccator with a saturated K₂CO₃ solution. The CVMs were characterized via SEM microscopy, cell adherence, FTIR, and manipulation in an ex vivo model. A pilot transplantation of the CECs/CVM construct in rabbits was also carried out. The thickness of the CVMs was 3.65–7.2 µm. The transparency was superior to a human cornea (92.6% = 1X; 94% = 2X; 89.21% = 3X). SEM microscopy showed a homogenous surface and laminar organization. The cell concentration seeded over the CVM increased threefold with no significant difference between 1X, 2X, and 3X (p = 0.323). The 2X-CVM was suitable for surgical manipulation in the ex vivo model. Constructs using the CECs/2X-CVM promoted corneal transparency restoration. Full article

(This article belongs to the Special Issue Multi-Functional Collagen-Based Biomaterials for Biomedical Applications)

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17 pages, 4604 KiB

Open AccessArticle

Collagen Membrane Derived from Fish Scales for Application in Bone Tissue Engineering

by Liang Chen, Guoping Cheng, Shu Meng and Yi Ding

Polymers 2022, 14(13), 2532; https://doi.org/10.3390/polym14132532 - 21 Jun 2022

Cited by 20 | Viewed by 3781

Abstract

Guided tissue/bone regeneration (GTR/GBR) is currently the main treatment for alveolar bone regeneration. The commonly used barrier membranes in GTR/GBR are collagen membranes from mammals such as porcine or cattle. Fish collagen is being explored as a potential substitute for mammalian collagen due to its low cost, no zoonotic risk, and lack of religious constraints. Fish scale is a multi-layer natural collagen composite with high mechanical strength, but its biomedical application is limited due to the low denaturation temperature of fish collagen. In this study, a fish scale collagen membrane with a high denaturation temperature of 79.5 °C was prepared using an improved method based on preserving the basic shape of fish scales. The fish scale collagen membrane was mainly composed of type I collagen and hydroxyapatite, in which the weight ratios of water, organic matter, and inorganic matter were 20.7%, 56.9%, and 22.4%, respectively. Compared to the Bio-Gide^® membrane (BG) commonly used in the GTR/GBR, fish scale collagen membrane showed good cytocompatibility and could promote late osteogenic differentiation of cells. In conclusion, the collagen membrane prepared from fish scales had good thermal stability, cytocompatibility, and osteogenic activity, which showed potential for bone tissue engineering applications. Full article

(This article belongs to the Special Issue Multi-Functional Collagen-Based Biomaterials for Biomedical Applications)

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21 pages, 8046 KiB

Open AccessArticle

Aquaponics-Derived Tilapia Skin Collagen for Biomaterials Development

by Nunzia Gallo, Maria Lucia Natali, Alessandra Quarta, Antonio Gaballo, Alberta Terzi, Teresa Sibillano, Cinzia Giannini, Giuseppe Egidio De Benedetto, Paola Lunetti, Loredana Capobianco, Federica Stella Blasi, Alessandro Sicuro, Angelo Corallo, Alessandro Sannino and Luca Salvatore

Polymers 2022, 14(9), 1865; https://doi.org/10.3390/polym14091865 - 2 May 2022

Cited by 16 | Viewed by 4115

Abstract

Collagen is one of the most widely used biomaterials in health-related sectors. The industrial production of collagen mostly relies on its extraction from mammals, but several issues limited its use. In the last two decades, marine organisms attracted interest as safe, abundant, and alternative source for collagen extraction. In particular, the possibility to valorize the huge quantity of fish industry waste and byproducts as collagen source reinforced perception of fish collagen as eco-friendlier and particularly attractive in terms of profitability and cost-effectiveness. Especially fish byproducts from eco-sustainable aquaponics production allow for fish biomass with additional added value and controlled properties over time. Among fish species, Oreochromis niloticus is one of the most widely bred fish in large-scale aquaculture and aquaponics systems. In this work, type I collagen was extracted from aquaponics-raised Tilapia skin and characterized from a chemical, physical, mechanical, and biological point of view in comparison with a commercially available analog. Performed analysis confirmed that the proprietary process optimized for type I collagen extraction allowed to isolate pure native collagen and to preserve its native conformational structure. Preliminary cellular studies performed with mouse fibroblasts indicated its optimal biocompatibility. All data confirmed the eligibility of the extracted Tilapia-derived native type I collagen as a biomaterial for healthcare applications. Full article

(This article belongs to the Special Issue Multi-Functional Collagen-Based Biomaterials for Biomedical Applications)

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14 pages, 2218 KiB

Open AccessArticle

Variation in Hydrogel Formation and Network Structure for Telo-, Atelo- and Methacrylated Collagens

by Malachy Kevin Maher, Jacinta F. White, Veronica Glattauer, Zhilian Yue, Timothy C. Hughes, John A. M. Ramshaw and Gordon G. Wallace

Polymers 2022, 14(9), 1775; https://doi.org/10.3390/polym14091775 - 27 Apr 2022

Cited by 8 | Viewed by 2548

Abstract

As the most abundant protein in the extracellular matrix, collagen has become widely studied in the fields of tissue engineering and regenerative medicine. Of the various collagen types, collagen type I is the most commonly utilised in laboratory studies. In tissues, collagen type I forms into fibrils that provide an extended fibrillar network. In tissue engineering and regenerative medicine, little emphasis has been placed on the nature of the network that is formed. Various factors could affect the network structure, including the method used to extract collagen from native tissue, since this may remove the telopeptides, and the nature and extent of any chemical modifications and crosslinking moieties. The structure of any fibril network affects cellular proliferation and differentiation, as well as the overall modulus of hydrogels. In this study, the network-forming properties of two distinct forms of collagen (telo- and atelo-collagen) and their methacrylated derivatives were compared. The presence of the telopeptides facilitated fibril formation in the unmodified samples, but this benefit was substantially reduced by subsequent methacrylation, leading to a loss in the native self-assembly potential. Furthermore, the impact of the methacrylation of the collagen, which enables rapid crosslinking and makes it suitable for use in 3D printing, was investigated. The crosslinking of the methacrylated samples (both telo- and atelo-) was seen to improve the fibril-like network compared to the non-crosslinked samples. This contrasted with the samples of methacrylated gelatin, which showed little, if any, fibrillar or ordered network structure, regardless of whether they were crosslinked. Full article

(This article belongs to the Special Issue Multi-Functional Collagen-Based Biomaterials for Biomedical Applications)

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Review

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39 pages, 2906 KiB

Open AccessReview

An Update on the Clinical Efficacy and Safety of Collagen Injectables for Aesthetic and Regenerative Medicine Applications

by Luca Salvatore, Maria Lucia Natali, Chiara Brunetti, Alessandro Sannino and Nunzia Gallo

Polymers 2023, 15(4), 1020; https://doi.org/10.3390/polym15041020 - 17 Feb 2023

Cited by 13 | Viewed by 17817

Abstract

Soft tissues diseases significantly affect patients quality of life and usually require targeted, costly and sometimes constant interventions. With the average lifetime increase, a proportional increase of age-related soft tissues diseases has been witnessed. Due to this, the last two decades have seen a tremendous demand for minimally invasive one-step resolutive procedures. Intensive scientific and industrial research has led to the recognition of injectable formulations as a new advantageous approach in the management of complex diseases that are challenging to treat with conventional strategies. Among them, collagen-based products are revealed to be one of the most promising among bioactive biomaterials-based formulations. Collagen is the most abundant structural protein of vertebrate connective tissues and, because of its structural and non-structural role, is one of the most widely used multifunctional biomaterials in the health-related sectors, including medical care and cosmetics. Indeed, collagen-based formulations are historically considered as the “gold standard” and from 1981 have been paving the way for the development of a new generation of fillers. A huge number of collagen-based injectable products have been approved worldwide for clinical use and have routinely been introduced in many clinical settings for both aesthetic and regenerative surgery. In this context, this review article aims to be an update on the clinical outcomes of approved collagen-based injectables for both aesthetic and regenerative medicine of the last 20 years with an in-depth focus on their safety and effectiveness for the treatment of diseases of the integumental, gastrointestinal, musculoskeletal, and urogenital apparatus. Full article

(This article belongs to the Special Issue Multi-Functional Collagen-Based Biomaterials for Biomedical Applications)

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13 pages, 577 KiB

Open AccessReview

Tissue Engineering with Stem Cell from Human Exfoliated Deciduous Teeth (SHED) and Collagen Matrix, Regulated by Growth Factor in Regenerating the Dental Pulp

by Vinna K. Sugiaman, Rudy Djuanda, Natallia Pranata, Silvia Naliani, Wayan L. Demolsky and Jeffrey

Polymers 2022, 14(18), 3712; https://doi.org/10.3390/polym14183712 - 6 Sep 2022

Cited by 11 | Viewed by 4922

Abstract

Maintaining dental pulp vitality and preventing tooth loss are two challenges in endodontic treatment. A tooth lacking a viable pulp loses its defense mechanism and regenerative ability, making it more vulnerable to severe damage and eventually necessitating extraction. The tissue engineering approach has drawn attention as an alternative therapy as it can regenerate dentin-pulp complex structures and functions. Stem cells or progenitor cells, extracellular matrix, and signaling molecules are triad components of this approach. Stem cells from human exfoliated deciduous teeth (SHED) are a promising, noninvasive source of stem cells for tissue regeneration. Not only can SHEDs regenerate dentin-pulp tissues (comprised of fibroblasts, odontoblasts, endothelial cells, and nerve cells), but SHEDs also possess immunomodulatory and immunosuppressive properties. The collagen matrix is a material of choice to provide structural and microenvironmental support for SHED-to-dentin pulp tissue differentiation. Growth factors regulate cell proliferation, migration, and differentiation into specific phenotypes via signal-transduction pathways. This review provides current concepts and applications of the tissue engineering approach, especially SHEDs, in endodontic treatment. Full article

(This article belongs to the Special Issue Multi-Functional Collagen-Based Biomaterials for Biomedical Applications)

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