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1.
Cureus ; 16(4): e58352, 2024 Apr.
Article in English | MEDLINE | ID: mdl-38756283

ABSTRACT

In the digital era, healthcare customer feedback plays a pivotal role in shaping the reputation of healthcare organizations. The study explores how digital advancements are integrated into modern healthcare, offering both transformative insights and addressing the challenges they present. It investigates how technologies such as artificial intelligence (AI), digital platforms, and patient feedback systems impact patient care, operational efficiency, and customer satisfaction in healthcare settings. The study emphasizes the importance of balancing both capitalizing on the opportunities presented by innovations and addressing the inherent difficulties associated with digitalization in healthcare, underlining the need for a comprehensive approach to navigating the opportunities and challenges in healthcare digitalization. AI is recognized for its role in reshaping value creation in healthcare, fostering collaboration among stakeholders, and improving patient care. Additionally, the study identifies key areas of research essential for effectively navigating the digital transformation in healthcare, including operational efficiency, patient-centric strategies, and organizational factors. However, along with the potential benefits come challenges, such as the need for regulatory frameworks to validate new technologies and address privacy concerns surrounding patient data. Managing reputation and customer relationships in the digital sphere also emerges as critical for healthcare organizations. In summary, the study underscores the importance of healthcare institutions prioritizing patient-centric care, adopting digital innovations, and adeptly navigating regulatory and ethical challenges. By doing so, they can enhance patient outcomes, and satisfaction, and drive innovation in today's dynamic healthcare landscape.

2.
J Biomed Mater Res A ; 105(4): 1112-1122, 2017 04.
Article in English | MEDLINE | ID: mdl-28093865

ABSTRACT

Poly(ethylene glycol) (PEG) hydrogels provide a versatile platform to develop cell instructive materials through incorporation of a variety of cell adhesive ligands and degradable chemistries. Synthesis of PEG gels can be accomplished via two mechanisms: chain and step growth polymerizations. The mechanism dramatically impacts hydrogel nanostructure, whereby chain polymerized hydrogels are highly heterogeneous and step growth networks exhibit more uniform structures. Underpinning these alterations in nanostructure of chain polymerized hydrogels are densely-packed hydrophobic poly(methyl methacrylate) or poly(acrylate) kinetic chains between hydrophilic PEG crosslinkers. As cell-material interactions, such as those mediated by integrins, occur at the nanoscale and affect cell behavior, it is important to understand how different modes of polymerization translate into nanoscale mechanical and hydrophobic heterogeneities of hydrogels. Therefore, chain- and step-growth polymerized PEG hydrogels with macroscopically similar macromers and compliance (for example, methacrylate-functionalized PEG (PEGDM), MW = 10 kDa and norbornene-functionalized 4-arm PEG (PEGnorb), MW = 10 kDa) were used to examine potential nanoscale differences in hydrogel mechanics and hydrophobicity using atomic force microscopy (AFM). It was found that chain-growth polymerized network yielded greater heterogeneities in both stiffness and hydrophobicity as compared to step-growth polymerized networks. These nanoscale heterogeneities impact cell-material interactions, particularly human mesenchymal stem cell (hMSC) adhesion and spreading, which has implications in use of these hydrogels for tissue engineering applications. © 2017 Wiley Periodicals, Inc. J Biomed Mater Res Part A: 105A: 1112-1122, 2017.


Subject(s)
Acrylic Resins , Hydrogels , Materials Testing , Mesenchymal Stem Cells/metabolism , Polyethylene Glycols , Polymethyl Methacrylate , Acrylic Resins/chemistry , Acrylic Resins/pharmacology , Humans , Hydrogels/chemistry , Hydrogels/pharmacology , Mesenchymal Stem Cells/cytology , Polyethylene Glycols/chemistry , Polyethylene Glycols/pharmacology , Polymethyl Methacrylate/chemistry , Polymethyl Methacrylate/pharmacology
3.
Chem Commun (Camb) ; 51(56): 11260-3, 2015 Jun 30.
Article in English | MEDLINE | ID: mdl-26081605

ABSTRACT

Fmoc-3F-Phe-Arg-NH2 and Fmoc-3F-Phe-Asp-OH dipeptides undergo coassembly to form two-component nanofibril hydrogels. These hydrogels support the viability and growth of NIH 3T3 fibroblast cells. The supramolecular display of Arg and Asp at the nanofibril surface effectively mimics the integrin-binding RGD peptide of fibronectin, without covalent connection between the Arg and Asp functionality.


Subject(s)
Biomimetic Materials/chemistry , Cell Culture Techniques/methods , Dipeptides/chemistry , Extracellular Matrix/chemistry , Fibroblasts/cytology , Hydrogels/chemistry , Animals , Biomimetics , Cell Survival , Mice , Models, Molecular , Molecular Conformation , NIH 3T3 Cells , Nanofibers/chemistry
4.
Langmuir ; 29(39): 12183-93, 2013 Oct 01.
Article in English | MEDLINE | ID: mdl-23968193

ABSTRACT

Thermoresponsive poly(N-isopropyl acrylamide) (PNIPAM) microgels were patterned on polystyrene substrates via dip coating, creating cytocompatible substrates that provided spatial control over cell adhesion. This simple dip-coating method, which exploits variable substrate withdrawal speeds forming particle suspension stripes of densely packed PNIPAM microgels, while spacings between the stripes contained sparsely distributed PNIPAM microgels. The assembly of three different PNIPAM microgel patterns, namely, patterns composed of 50 µm stripe/50 µm spacing, 50 µm stripe/100 µm spacing, and 100 µm stripe/100 µm spacing, was verified using high-resolution optical micrographs and ImageJ analysis. PNIPAM microgels existed as monolayers within stripes and spacings, as revealed by atomic force microscopy (AFM). Upon cell seeding on PNIPAM micropatterned substrates, NIH3T3 fibroblast cells preferentially adhered within spacings to form cell patterns. Three days after cell seeding, cells proliferated to form confluent cell layers. The thermoresponsiveness of the underlying PNIPAM microgels was then utilized to recover fibroblast cell sheets from substrates simply by lowering the temperature without disrupting the underlying PNIPAM microgel patterns. Harvested cell sheets similar to these have been used for multiple tissue engineering applications. Also, this simple, low-cost, template-free dip-coating technique can be utilized to micropattern multifunctional PNIPAM microgels, generating complex stimuli-responsive substrates to study cell-material interactions and allow drug delivery to cells in a spatially and temporally controlled manner.


Subject(s)
Acrylic Resins/chemistry , Fibroblasts/cytology , Gels/chemistry , Temperature , Acrylic Resins/chemical synthesis , Animals , Cell Adhesion , Mice , NIH 3T3 Cells , Particle Size , Surface Properties
5.
Tissue Eng Part B Rev ; 19(6): 455-69, 2013 Dec.
Article in English | MEDLINE | ID: mdl-23541134

ABSTRACT

For many tissue engineering applications and studies to understand how materials fundamentally affect cellular functions, it is important to have the ability to synthesize biomaterials that can mimic elements of native cell-extracellular matrix interactions. Hydrogels possess many properties that are desirable for studying cell behavior. For example, hydrogels are biocompatible and can be biochemically and mechanically altered by exploiting the presentation of cell adhesive epitopes or by changing hydrogel crosslinking density. To establish physical and biochemical tunability, hydrogels can be engineered to alter their properties upon interaction with external driving forces such as pH, temperature, electric current, as well as exposure to cytocompatible irradiation. Additionally, hydrogels can be engineered to respond to enzymes secreted by cells, such as matrix metalloproteinases and hyaluronidases. This review details different strategies and mechanisms by which biomaterials, specifically hydrogels, can be manipulated dynamically to affect cell behavior. By employing the appropriate combination of stimuli and hydrogel composition and architecture, cell behavior such as adhesion, migration, proliferation, and differentiation can be controlled in real time. This three-dimensional control in cell behavior can help create programmable cell niches that can be useful for fundamental cell studies and in a variety of tissue engineering applications.


Subject(s)
Cells/cytology , Cells/drug effects , Hydrogels/chemistry , Hydrogels/pharmacology , Materials Testing , Animals , Humans
6.
ACS Chem Biol ; 5(4): 393-403, 2010 Apr 16.
Article in English | MEDLINE | ID: mdl-20175560

ABSTRACT

Protein organization on biomembranes and their dynamics are essential for cellular function. It is not clear, however, how protein binding may influence the assembly of underlying lipids or how the membrane structure leads to functional protein organization. Toward this goal, we investigated the effects of annexin a5 binding to biomimetic membranes using fluorescence imaging and correlation spectroscopy. Annexin a5 (anx a5), a peripheral intracellular protein that plays a membrane remodeling role in addition to other functions, binds specifically and tightly to anionic (e.g., phosphatidylserine)-containing membranes in the presence of calcium ion. Our fluorescence microscopy reveals that annexin likely forms assemblies, along with a more dispersed population, upon binding to anionic biomembranes in the presence of calcium ion, which is reflected in its two-component Brownian motion. To investigate the effects of annexin binding on the underlying lipids, we used specific acyl chain labeled phospholipid analogues, NBD-phosphatidylcholine (NBD-PC) and NBD-phosphatidylserine (NBD-PS). We find that both NBD-labeled lipids cluster under anx a5 assemblies, as compared with when they are found under the dispersed annexin population, and NBD-PS exhibits two-component lateral diffusion under the annexin assemblies. In contrast, NBD-PC diffusion is slower by an order of magnitude under the annexin assemblies in contrast to its diffusion when not localized under anx a5 assemblies. Our results indicate that, upon binding to membranes, the peripheral protein annexin organizes the underlying lipids into domains, which may have functional implications in vivo.


Subject(s)
Annexin A5/metabolism , Lipid Bilayers/metabolism , Annexin A5/chemistry , Calcium/metabolism , Diffusion , Lipid Bilayers/chemistry , Membranes, Artificial , Microscopy, Fluorescence , Phosphatidylserines/chemistry , Phosphatidylserines/metabolism , Protein Binding , Protein Conformation , Spectrometry, Fluorescence
7.
Biochim Biophys Acta ; 1778(11): 2461-8, 2008 Nov.
Article in English | MEDLINE | ID: mdl-18703013

ABSTRACT

Biomembranes are complex, heterogeneous, dynamic systems playing essential roles in numerous processes such as cell signaling and membrane trafficking. Model membranes provide simpler platforms for studying biomembrane dynamics under well-controlled environments. Here we present a modified polymer lift-off approach to introduce chemical complexity into biomimetic membranes by constructing domains of one lipid composition (here, didodecylphosphatidylcholine) that are surrounded by a different lipid composition (e.g., dipentadecylphosphatidylcholine), which we refer to as patterned backfilled samples. Fluorescence microscopy and correlation spectroscopy were used to characterize this patterning approach. We observe two types of domain populations: one with diffuse boundaries and a minor fraction with sharp edges. Lipids within the diffuse domains in patterned backfilled samples undergo anomalous diffusion, which results from nonideally mixed clusters of gel phase lipid within the fluid domains. No lateral diffusion was observed within the minor population of domains with well-defined borders. These results suggest that, while membrane patterning by a variety of approaches is useful for biophysical and biosensor applications, a thorough and systematic characterization of the resulting biomimetic membrane, and its unpatterned counterpart, is essential.


Subject(s)
Membranes, Artificial , Boron Compounds , Diffusion , Fluorescence , Lipids/chemistry , Microscopy, Atomic Force , Phosphatidylcholines/chemistry , Polymers/chemistry , Unilamellar Liposomes/chemistry
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