Jeffrey D Hartgerink

Rice University, Houston, Texas, United States

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Publications (73)593.35 Total impact

  • Vivek A. Kumar · Navindee C. Wickremasinghe · Siyu Shi · Jeffrey D. Hartgerink ·

    10/2015; DOI:10.1021/acsbiomaterials.5b00356
  • Navindee C. Wickremasinghe · Vivek A. Kumar · Siyu Shi · Jeffrey D. Hartgerink ·

    09/2015; 1(9):845-854. DOI:10.1021/acsbiomaterials.5b00210
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    ABSTRACT: Delivery of small molecules and drugs to tissues is a mainstay of several tissue engineering strategies. Next generation treatments focused on localized drug delivery offer a more effective means in dealing with refractory healing when compared to systemic approaches. Here we describe a novel multidomain peptide hydrogel that capitalizes on synthetic peptide chemistry, supramolecular self-assembly and cytokine delivery to tailor biological responses. This material is biomimetic, shows shear stress recovery and offers a nanofibrous matrix that sequesters cytokines. The biphasic pattern of cytokine release results in the spatio-temporal activation of THP-1 monocytes and macrophages. Furthermore, macrophage-material interactions are promoted without generation of a proinflammatory environment. Subcutaneous implantation of injectable scaffolds showed a marked increase in macrophage infiltration and polarization dictated by cytokine loading as early as 3 days, with complete scaffold resorption by day 14. Macrophage interaction and response to the peptide composite facilitated the (i) recruitment of monocytes/macrophages, (ii) sustained residence of immune cells until degradation, and (iii) promotion of a pro-resolution M2 environment. Our results suggest the potential use of this injectable cytokine loaded hydrogel scaffold in a variety of tissue engineering applications. Copyright © 2015 Elsevier Ltd. All rights reserved.
    Biomaterials 06/2015; 52(1). DOI:10.1016/j.biomaterials.2015.01.079 · 8.56 Impact Factor
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    ABSTRACT: Self-assembly of multidomain peptides (MDP) can be tailored to carry payloads that modulate the extracellular environment. Controlled release of growth factors, cytokines, and small-molecule drugs allows for unique control of in vitro and in vivo responses. In this study, we demonstrate this process of ionic cross-linking of peptides using multivalent drugs to create hydrogels for sustained long-term delivery of drugs. Using phosphate, heparin, clodronate, trypan, and suramin, we demonstrate the utility of this strategy. Although all multivalent anions result in good hydrogel formation, demonstrating the generality of this approach, suramin led to the formation of the best hydrogels per unit concentration and was studied in greater detail. Suramin ionically cross-linked MDP into a fibrous meshwork as determined by scanning and transmission electron microscopy. We measured material storage and loss modulus using rheometry and showed a distinct increase in G' and G″ as a function of suramin concentration. Release of suramin from scaffolds was determined using UV spectroscopy and showed prolonged release over a 30 day period. Suramin bioavailability and function were demonstrated by attenuated M1 polarization of THP-1 cells compared to positive control. Overall, this design strategy has allowed for the development of a novel class of polymeric delivery vehicles with generally long-term release and, in the case of suramin, cross-linked hydrogels that can modulate cellular phenotype.
    Journal of the American Chemical Society 04/2015; 137(14). DOI:10.1021/jacs.5b01549 · 12.11 Impact Factor
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    ABSTRACT: Major limitations of current tissue regeneration approaches using artificial scaffolds are fibrous encapsulation, lack of host cellular infiltration, unwanted immune responses, surface degradation preceding biointegration, and artificial degradation byproducts. Specifically, for scaffolds larger than 200-500 μm, implants must be accompanied by host angiogenesis in order to provide adequate nutrient/waste exchange in the newly forming tissue. In the current work, we design a peptide-based self-assembling nanofibrous hydrogel containing cell-mediated degradation and proangiogenic moieties that specifically address these challenges. This hydrogel can be easily delivered by syringe, is rapidly infiltrated by cells of hematopoietic and mesenchymal origin, and rapidly forms an extremely robust mature vascular network. Scaffolds show no signs of fibrous encapsulation and after 3 weeks are resorbed into the native tissue. These supramolecular assemblies may prove a vital paradigm for tissue regeneration and specifically for ischemic tissue disease.
    ACS Nano 01/2015; 9(1). DOI:10.1021/nn506544b · 12.88 Impact Factor
  • Amanda M Acevedo-Jake · Abhishek A Jalan · Jeffrey D Hartgerink ·
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    ABSTRACT: The collagen triple helix consists of three supercoiled solvent-exposed polypeptide chains, and by dry weight it is the most abundant fold in mammalian tissues. Many factors affecting the structure and stability of collagen have been determined through the use of short synthetically prepared peptides, generally called collagen-mimetic peptides (CMPs). NMR (nuclear magnetic resonance spectroscopy) investigations into the molecular structure of CMPs have suffered from large amounts of signal overlap and degeneracy because of collagen's repetitive primary sequence, the close and symmetric packing of the three chains and the identical peptide sequences found in homotrimers. In this paper a peptide library is prepared in which a single isotopic (15)N-Gly label is moved sequentially along the peptide backbone. Our approach allows for a more explicit examination of local topology than available in past reports. This reveals larger regions of disorder at the C-terminus than previously detected by crystallographic or NMR studies, and here C-terminal fraying is seen to extend for six amino acids in a (POG)10 sequence. Furthermore, small sequence changes at the N-terminus greatly influence the degree of this localized disorder and may be useful in the future design of CMPs to maximize collagen's interstrand hydrogen bonding pattern. Our approach and data serves as a reference for future CMP characterizations to determine the quality and extent of folding.
    Biomacromolecules 01/2015; 16(1):145-55. DOI:10.1021/bm501281a · 5.75 Impact Factor
  • Biplab Sarkar · Lesley E R O'Leary · Jeffrey D Hartgerink ·
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    ABSTRACT: Mimicking the multistep self-assembly of the fibrillar protein collagen is an important design challenge in biomimetic supramolecular chemistry. Utilizing the complementarity of oppositely charged domains in short collagen-like peptides, we have devised a strategy for the self-assembly of these peptides into fibers. The strategy depends on the formation of a staggered triple helical species facilitated by interchain charged pairs, and is inspired by similar sticky-ended fibrillation designs applied in DNA and coiled coil fibers. We compare two classes of collagen mimetic peptides with the same composition but different domain arrangements, and show that differences in their proposed nucleation events differentiates their fibrillation capabilities. Larger nucleation domains result in rapid fiber formation and eventual precipitation or gelation while short nucleation domains leave the peptide soluble for long periods of time. For one of the fiber-forming peptides, we elucidate the packing parameters by X-ray diffraction.
    Journal of the American Chemical Society 10/2014; 136(41):14417-14424. DOI:10.1021/ja504377s · 12.11 Impact Factor
  • Source
    Navindee C Wickremasinghe · Vivek A Kumar · Jeffrey D Hartgerink ·
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    ABSTRACT: Progress in self-assembly and supramolecular chemistry has been directed toward obtaining macromolecular assemblies with higher degrees of complexity, simulating the highly structured environment in natural systems. One approach to this type of complexity are multistep, multicomponent, self-assembling systems that allow approaches comparable to traditional multistep synthetic organic chemistry; however, only a few examples of this approach have appeared in the literature. Our previous work demonstrated nanofibrous mimics of the extracellular matrix. Here we demonstrate the ability to create a unique hydrogel, developed by stepwise self-assembly of multidomain peptide fibers and liposomes. The two-component system allows for controlled release of bioactive factors at multiple time points. The individual components of the self-assembled gel and the composite hydrogel were characterized by TEM, SEM, and rheometry, demonstrating that peptide nanofibers and lipid vesicles both retain their structural integrity in the composite gel. The rheological robustness of the hydrogel is shown to be largely unaffected by the presence of liposomes. Release studies from the composite gels loaded with different growth factors EGF, MCP-1, and PlGF-1 showed delay and prolongation of release by liposomes entrapped in the hydrogel compared to more rapid release from the hydrogel alone. This bimodal release system may have utility in systems where timed cascades of biological signals may be valuable, such as in tissue regeneration.
    Biomacromolecules 10/2014; 15(10):3587-95. DOI:10.1021/bm500856c · 5.75 Impact Factor
  • Abhishek A Jalan · Katherine A Jochim · Jeffrey D Hartgerink ·
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    ABSTRACT: In a canonical collagen triple helix, three peptides self-assemble into a supercoiled motif with a one-amino-acid offset between the peptide chains. Design of triple helices that contain more than one residue offset is lucrative, as it leaves the non-covalent interactions unsatisfied at the termini and renders the termini "sticky" to further self-assemble into collagen-like nanofibers. Here we use lysine-glutamate axial salt-bridges to design a heterotrimeric collagen triple helix, ABC-1, containing a non-canonical offset of four residues between the peptide chains. The four-residue offset is necessary to prevent aggregation, which would prevent characterization of the non-canonical chain arrangement at the molecular level by NMR spectroscopy. A second heterotrimer, ABC-2, also stabilized by axial salt-bridges, is designed containing a canonical one-amino-acid offset to facilitate comparison of structure and stability by CD and NMR. ABC-1 and ABC-2 demonstrate our ability to modulate chain offset in a collagen triple helix. This lays the groundwork to design longer, and therefore stickier, offsets allowing access to a new class of collagen-related nanostructures.
    Journal of the American Chemical Society 05/2014; 136(21). DOI:10.1021/ja5001246 · 12.11 Impact Factor
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    Marci K Kang · John S Colombo · Rena N D'Souza · Jeffrey D Hartgerink ·
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    ABSTRACT: Here we report three new nanofibrous, self-assembling multidomain peptide (MDP) sequences and examine the effect of sequence on the morphology and expansion of encapsulated Stem cells from Human Exfoliated Deciduous teeth (SHED). We modified our previously reported set of serine-based MDPs, changing the serine residues in the amphiphilic region to threonine. The three new threonine-based sequences self-assemble into antiparallel β-sheet nanofibers, confirmed by CD and IR. AFM and negative-stained TEM show that the nanofibers formed by the new sequences are more curved than their serine-containing predecessors. Despite this change in nanofiber morphology, SEM illustrates that all three new sequences still form porous hydrogels. K(TL)2SLRG(TL)3KGRGDS, with a designed cleavage site, is able to be degraded by Matrix Metalloprotease 2. We then examine SHED cell response to these new sequences as well as their serine-based predecessors. We observe faster cell attachment and spreading in hydrogels formed by K2(SL)6K2GRGDS and K(SL)3RG(SL)3KGRGDS. By day 3, the SHEDs in all of the serine-based sequences exhibit a fibroblast-like morphology. Additionally, the SHED cells expand more rapidly in the serine-based gels while the cell number remains relatively constant in the threonine-based peptides. In hydrogels formed by K2(TL)6K2GRGDS and K(TL)2SLRG(TL)3KGRGDS, this low expansion rate is accompanied by changes in morphology where SHEDs exhibit a stellate morphology after 3 days in culture; however, by day 7 they appear more fibroblast-shaped. Throughout the duration of the experiment, the SHED cells encapsulated in the K2(TL)6K2 hydrogels remain rounded. These results suggest that the basic MDP structure easily accommodates modifications in sequence and, for SHED cells, the threonine-containing gels require the integrin-binding RGDS sequence for cell attachment to occur, while the serine-based gels are less selective and support an increase in cell number, regardless of the presence or absence of RGDS.
    Biomacromolecules 05/2014; 15(6). DOI:10.1021/bm500075r · 5.75 Impact Factor
  • John S. Colombo · Amanda N. Moore · Jeffrey D. Hartgerink · Rena N. D’Souza ·
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    ABSTRACT: In dentistry, the maintenance of a vital dental pulp is of paramount importance because teeth devitalized by root canal treatment may become more brittle and prone to structural failure over time. Advanced carious lesions can irreversibly damage the dental pulp by propagating a sustained inflammatory response throughout the tissue. Although the inflammatory response initially drives tissue repair, sustained inflammation has an enormously destructive effect on the vital pulp, eventually leading to total necrosis of the tissue and necessitating its removal. The implications of tooth devitalization have driven significant interest in the development of bioactive materials that facilitate the regeneration of damaged pulp tissues by harnessing the capacity of the dental pulp for self-repair. In considering the process by which pulpitis drives tissue destruction, it is clear that an important step in supporting the regeneration of pulpal tissues is the attenuation of inflammation. Macrophages, key mediators of the immune response, may play a critical role in the resolution of pulpitis because of their ability to switch to a proresolution phenotype. This process can be driven by the resolvins, a family of molecules derived from fatty acids that show great promise as therapeutic agents. In this review, we outline the importance of preserving the capacity of the dental pulp to self-repair through the rapid attenuation of inflammation. Potential treatment modalities, such as shifting macrophages to a proresolving phenotype with resolvins are described, and a range of materials known to support the regeneration of dental pulp are presented.
    Journal of endodontics 04/2014; 40(4):S6–S12. DOI:10.1016/j.joen.2014.01.019 · 3.38 Impact Factor
  • Abhishek A Jalan · Jeffrey D Hartgerink ·
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    ABSTRACT: A comprehensive survey of single amino acid substitutions in the canonical Xaa-Yaa-Gly repeat has laid the ground work for our understanding of the collagen triple helix. Building upon this foundation requires understanding pairwise amino acid interactions which will allow us to prepare heterotrimeric helices with great specificity in addition to an overall improved control over helix structure and stability. Furthermore, detailed studies on these interactions will help us understand collagen's n structure, assembly mechanism and stability. The most important pairwise interaction so far identified in the collagen triple helix is the axial charge pair that can be formed between properly placed Lysine and either Aspartate or Glutamate residues. This review will summarize our understanding of this interaction and other charged pair interactions and how they have been successfully used to control collagen triple helix self-assembly.
    Current opinion in chemical biology 11/2013; 17(6). DOI:10.1016/j.cbpa.2013.10.019 · 6.81 Impact Factor
  • Abhishek A Jalan · Borries Demeler · Jeffrey Dale Hartgerink ·
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    ABSTRACT: Hydroxyproline plays a major role in stabilizing collagenous domains in eukaryotic organisms. Lack of this modification is associated with significant lowering in thermal stability of the collagen triple helix and may also affect fibrillogenesis and folding of the peptide chains. In contrast, even though bacterial collagens lack hydroxyproline, their thermal stability is comparable to fibrillar collagen. This has been attributed to the high frequency of charged amino acids found in bacterial collagen. Here we report a thermally stable hydroxyproline-free ABC heterotrimeric collagen mimetic system composed of decapositive and decanegative peptides and a zwitterionic peptide. None of the peptides contain hydroxyproline and furthermore the zwitterionic peptide does not even contain proline. The heterotrimer is electrostatically stabilized via multiple interpeptide lysine-aspartate and lysine- glutamate salt-bridges and maintains good thermal stability with a melting temperature of 37 °C. The ternary peptide mixture also populates a single composition ABC heterotrimer as confirmed by circular dichroism (CD) and Nuclear Magnetic Resonance (NMR) spectroscopy. This system illustrates the power of axial salt-bridges to direct and stabilize the self-assembly of a triple helix and may be useful in analogous designs in expression systems where the incorporation of hydroxyproline is challenging.
    Journal of the American Chemical Society 04/2013; 135(16). DOI:10.1021/ja402187t · 12.11 Impact Factor
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    Erica L Bakota · Ozge Sensoy · Beytullah Ozgur · Mehmet Sayar · Jeffrey Dale Hartgerink ·
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    ABSTRACT: Self-assembling multidomain peptides have been shown to have desirable properties, such as the ability to form hydrogels that rapidly recover following shear-thinning and the potential to be tailored by amino acid selection to vary their elasticity and encapsulate and deliver proteins and cells. Here we describe the effects of substitution of aliphatic hydrophobic amino acids in the central domain of the peptide for the aromatic amino acids phenylalanine, tyrosine and tryptophan. While the basic nanofibrous morphology is retained in all cases, selection of the particular core residues results in switching from anti-parallel hydrogen bonding to parallel hydrogen bonding in addition to changes in nanofiber morphology and in hydrogel rheological properties. Peptide nanofiber assemblies are investigated by circular dichroism polarimetry, infrared spectroscopy, atomic force microscopy, transmission and scanning electron microscopy, oscillatory rheology and molecular dynamics simulations. Results from this study will aid in designing next generation cell scaffolding materials.
    Biomacromolecules 03/2013; 14(5). DOI:10.1021/bm4000019 · 5.75 Impact Factor
  • Abhishek A Jalan · Jeffrey Dale Hartgerink ·
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    ABSTRACT: Control over composition and register of the peptide chains in AAB-type collagen mimetic heterotrimers is critical in developing systems that show fidelity to native collagen. However, their design is challenging due to the eight competing states possible for a mixture of non-identical peptides A and B. Interpeptide salt-bridges have been used previously as keystone in-teractions to bias the population of competing states to favor a target heterotrimer. The designed heterotrimers were electroneutral and relied on pairing of acidic and basic residues, but could not differentiate between all of the competing states and reported systems populated either multiple heterotrimer compositions or registers. Here our design methodology includes both positive and negative elements. First, an excess of acidic or basic residues, that always remain unpaired, in-troduces a negative design component to destabilize the competing triple helical compositions and registers. Second, charge pairs introduce a positive design component and stabilize the target assembly. These antagonistic factors are optimized in the target heterotrimer that forms the max-imum number of charge pairs and minimizes unpaired charged residues. Additionally, we find that not just the number of paired and unpaired residues are important, but also the type. By a systematic study of different types of charge pairs and unpaired residues we are able to populate a single composition-single register AAB heterotrimer. The insights gained here may be useful in designing composition and register specific heterotrimeric ligands with domains that recognize collagen-binding proteins.
    Biomacromolecules 12/2012; 14(1). DOI:10.1021/bm3015818 · 5.75 Impact Factor
  • Jorge A Fallas · Jeffrey D Hartgerink ·
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    ABSTRACT: The contribution of pairwise amino-acid interactions to the stability of collagen triple helices has remained elusive. Progress in this area is critical for the prediction of triple helical stability from sequences and the preparation of mimetic materials based on this fold. Here we report a sequence-based scoring function for triple helices that takes into account the stability conferred to collagen by axial lysine-aspartate salt bridges. This function is used to predict the stability of a specific register formed from three distinct peptide sequences and that of all alternative compositions and registers. In the context of a genetic algorithm we use it to select sequences likely to self-assemble with high stability and to the exclusion of the other 26 possible combinations. We validate our methodology by synthesis and structural characterization of the designed peptides, which self-assemble into a highly stable ABC triple helix with control over both composition and register.
    Nature Communications 09/2012; 3:1087. DOI:10.1038/ncomms2084 · 11.47 Impact Factor
  • Fang Wei · Jorge A Fallas · Jeffrey D Hartgerink ·
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    ABSTRACT: In this study, we examine eight ABC heterotrimers whose self-assembly is directed through electrostatic interactions. Oppositely charged pairs of amino acids, with varying side chain length, were assessed for their ability to stabilize a triple helix. Aspartate-lysine was found to result in the most thermally stable helix followed by lysine-glutamate, ornithine-aspartate, and finally ornithine-glutamate. When the sequence position of these charged amino acids was reversed from what is normally observed in nature, triple helix stability and compositional purity were significantly reduced. We examine the effect of salt on triple helix stability and observe that increased salt concentration reduces the thermal stability of heterotrimers by an average of 5 °C, but does not disrupt helix assembly. It was also found that some highly positively charged homotrimers can be stabilized in the presence of phosphate anions.
    Macromolecular Rapid Communications 09/2012; 33(17):1445-52. DOI:10.1002/marc.201200221 · 4.94 Impact Factor
  • Jorge A Fallas · Michael A Lee · Abhishek A Jalan · Jeffrey D Hartgerink ·
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    ABSTRACT: Design of heterotrimeric ABC collagen triple helices is challenging due to the large number of competing species that may be formed. Given the required one amino acid stagger between adjacent peptide strands in this fold, a ternary mixture of peptides can form as many as 27 triple helices with unique composition or register. Previously we have demonstrated that electrostatic interactions can be used to bias the helix population toward a desired target. However, homotrimeric assemblies have always remained the most thermally stable species in solution and therefore comprised a significant component of the peptide mixture. In this work we incorporate complementary modifications to this triple-helical design strategy to destabilize an undesirable competing state while compensating for this destabilization in the desired ABC composition. The result of these modifications is a new ABC triple-helical system with high thermal stability and control over composition, as observed by NMR. An additional set of modifications, which exchanges aspartate for glutamate, results in an overall lowering of stability of the ABC triple helix yet shows further improvement in the system's specificity. This rationally designed system helps to elucidate the rules governing the self-assembly of synthetic collagen triple helices and sheds light on the biological mechanisms of collagen assembly.
    Journal of the American Chemical Society 01/2012; 134(3):1430-3. DOI:10.1021/ja209669u · 12.11 Impact Factor
  • Source
    Jorge A Fallas · Jinhui Dong · Yizhi J Tao · Jeffrey D Hartgerink ·
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    ABSTRACT: The collagen triple helix is the most abundant protein fold in humans. Despite its deceptively simple structure, very little is understood about its folding and fibrillization energy landscape. In this work, using a combination of x-ray crystallography and nuclear magnetic resonance spectroscopy, we carry out a detailed study of stabilizing pair-wise interactions between the positively charged lysine and the negatively charged amino acids aspartate and glutamate. We find important differences in the side chain conformation of amino acids in the crystalline and solution state. Structures from x-ray crystallography may have similarities to the densely packed triple helices of collagen fibers whereas solution NMR structures reveal the simpler interactions of isolated triple helices. In solution, two distinct types of contacts are observed: axial and lateral. Such register-specific interactions are crucial for the understanding of the registration process of collagens and the overall stability of proteins in this family. However, in the crystalline state, there is a significant rearrangement of the side chain conformation allowing for packing interactions between adjacent helices, which suggests that charged amino acids may play a dual role in collagen stabilization and folding, first at the level of triple helical assembly and second during fibril formation.
    Journal of Biological Chemistry 12/2011; 287(11):8039-47. DOI:10.1074/jbc.M111.296574 · 4.57 Impact Factor
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    ABSTRACT: Recent successes in dental pulp engineering indicate that regenerative treatment strategies in endodontics are feasible. Clinically, revascularization procedures render completion of root formation in immature teeth. The generation of a pulp-like tissue after seeding of dental pulp stem cells into dentin discs or cylinders and transplantation in vivo is possible. In this experimental setup, which mimics the situation in the root canal, the pretreatment of dentin might influence cellular behavior at the cell-dentin interface. Thus, the objective of this study was to investigate whether dentin conditioning can determine cell fate. Dental pulp stem cells (DPSCs) were seeded into a growth factor-laden peptide hydrogel, transferred into dentin cylinders, and transplanted subcutaneously into immunocompromised mice. Before cell seeding, dentin cylinders were either pretreated with sodium hypochloride (NaOCl) or conditioned with EDTA. The constructs were explanted after 6 weeks and subjected to histological and immunohistochemical analysis. In dentin treated with NaOCl, resorption lacunae were found at the cell-dentin interface created by multinucleated cells with clastic activity. After conditioning with EDTA, DPSCs adjacent to the dentin formed an intimate association with the surface, differentiated into odontoblasts-like cells that expressed dentin sialoprotein, and extended cellular processes into the dentinal tubules. A vascularized soft connective tissue similar to dental pulp was observed inside the dentin cylinder. Dentin conditioning considerably influences DPSC fate when seeded in close proximity to dentin. This information might be critical for optimized strategic planning for future regenerative endodontic treatment.
    Journal of endodontics 11/2011; 37(11):1536-41. DOI:10.1016/j.joen.2011.08.027 · 3.38 Impact Factor

Publication Stats

4k Citations
593.35 Total Impact Points


  • 2005-2015
    • Rice University
      • • Department of Bioengineering
      • • Department of Chemistry
      Houston, Texas, United States
  • 2006
    • Newcastle University
      • Faculty of Medical Sciences
      Newcastle upon Tyne, ENG, United Kingdom
  • 2001-2003
    • Northwestern University
      • • Feinberg School of Medicine
      • • Department of Materials Science and Engineering
      Evanston, IL, United States