PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 21875751-3 2011 The pH-responsive synthetic mucin-like polymer is constructed with phenylboronic acid (PBA) and salicylhydroxamic acid (SHA), each individually copolymerized with a 2-hydroxypropyl methacrylamide (pHPMA) polymer backbone. Polymers 39-46 LOC100508689 Homo sapiens 28-33 19580278-4 2009 The novel rodlike polymers mimic the architecture of mucin glycoproteins and feature a phospholipid tail for membrane incorporation and a fluorescent optical probe for FLIC imaging situated at the opposite termini of the densely glycosylated polymeric backbones. Polymers 18-26 LOC100508689 Homo sapiens 53-58 20615996-4 2011 These mucus layers are organized around the highly glycosylated MUC2 mucin, forming a large, net-like polymer that is secreted by the goblet cells. Polymers 102-109 LOC100508689 Homo sapiens 69-74 19482258-8 2010 From various experimental methods on solutions of mucin it was found that at pH values around 2 (uncharged polymer), the intensive hydrophobic interactions lead to large association complexes, whereas at pH>>2 the negative charges suppress the tendency of forming associations. Polymers 107-114 LOC100508689 Homo sapiens 50-55 20441741-8 2010 We show that electrostatic interactions between diffusing particles and mucin polymers regulate the permeability properties of reconstituted mucin hydrogels. Polymers 78-86 LOC100508689 Homo sapiens 72-77 20441741-8 2010 We show that electrostatic interactions between diffusing particles and mucin polymers regulate the permeability properties of reconstituted mucin hydrogels. Polymers 78-86 LOC100508689 Homo sapiens 141-146 19950890-0 2010 PGSE-NMR and SANS studies of the interaction of model polymer therapeutics with mucin. Polymers 54-61 LOC100508689 Homo sapiens 80-85 19950890-2 2010 Pulsed-gradient spin-echo NMR and small-angle neutron scattering have been used to study the aqueous solution interaction of various model polymer therapeutics with mucin, the principle organic component within mucus. Polymers 139-146 LOC100508689 Homo sapiens 165-170 19950890-3 2010 Nonionic polymers such as linear and star-branched poly(ethylene oxide) (PEO) and dextrin showed no appreciable interaction with mucin but suffered a moderate retardation in their rate of diffusion through the mucin solution. Polymers 9-17 LOC100508689 Homo sapiens 210-215 19950890-5 2010 These observations have implications for the design of optimized polymer therapeutic structures being adopted for the delivery of therapeutic moieties through mucin-rich environments. Polymers 65-72 LOC100508689 Homo sapiens 159-164 17915910-5 2007 Data from two independent probes, fluorophores conjugated directly to the polymer backbone and fluorescent proteins bound to the sugar groups, unexpectedly show that the mucin mimic molecules lie flat along the membrane. Polymers 74-81 LOC100508689 Homo sapiens 170-175 19150404-4 2009 The new polymer Mc-MCC had swelling and moisture sorption profiles that were different from those of Mc and MCC in buffer solutions with different pH values and relative humidity, respectively. Polymers 8-15 LOC100508689 Homo sapiens 16-18 19150404-8 2009 The presence of new peaks in the FT-IR spectrum and distinct cold crystallization exotherm, which were absent in both Mc and MCC, confirms the formation of a new polymer type with synergistic physicochemical and functional properties. Polymers 162-169 LOC100508689 Homo sapiens 118-120 18720139-1 2008 To overcome the relatively short gastrointestinal (GI) time and improve localization for oral controlled or sustained release drug delivery systems, bioadhesive polymers that adhere to the mucin/epithelial surface are effective and lead to significant improvement in oral drug delivery. Polymers 161-169 LOC100508689 Homo sapiens 189-194 18291605-4 2008 Turbidimetric interaction between the aqueous dispersions of mucin and agarose was used to determine the concentration ratio of optimum interaction between the two polymers. Polymers 164-172 LOC100508689 Homo sapiens 61-66 18513929-7 2008 The mucoadhesive measurements were performed by tensile test and the bioadhesive bond between the polymer emulsifier and mucin was visualized by confocal laser scanning microscopy. Polymers 98-105 LOC100508689 Homo sapiens 121-126 12056529-2 2002 The capacity of some polymers to adhere to the mucin coat covering the conjunctiva and the corneal surface of the eye forms the basis for ocular mucoadhesion. Polymers 21-29 LOC100508689 Homo sapiens 47-52 16683774-1 2006 We developed a polymer coating for carbon nanotubes (CNTs) that mimics the mucin glycoprotein coating of mammalian cells. Polymers 15-22 LOC100508689 Homo sapiens 75-80 16683774-2 2006 CNTs coated with these mucin mimic polymers have two novel properties: they can bind to carbohydrate receptors, providing a means for biomimetic interactions with cell surfaces, and, importantly, they are rendered nontoxic to cells. Polymers 35-43 LOC100508689 Homo sapiens 23-28 16104759-0 2005 Combinatorial synthesis of MUC1 glycopeptides: polymer blotting facilitates chemical and enzymatic synthesis of highly complicated mucin glycopeptides. Polymers 47-54 LOC100508689 Homo sapiens 131-136 15262466-2 2005 However, for use as an artificial cornea, contact lens and in other applications, modifications with hydrophilic functional groups or polymers are necessary to improve wettability for tear protein and mucin interactions and to improve glucose permeability for cellular health. Polymers 134-142 LOC100508689 Homo sapiens 201-206 12202389-8 2002 The determined persistence length of the native mucin, 36 nm, is consistent with that of an extended, flexible polymer; such characteristics will influence the properties of the gels formed in vivo. Polymers 111-118 LOC100508689 Homo sapiens 48-53 17356062-6 2007 AFM analysis of mucin polymers at the single molecule level provides new information about the genetic origins of individual polymers and the contributions of glycosylation to the physicochemical properties of mucins, which can be correlated with information obtained from biochemistry, antibody binding assays, and molecular biology techniques. Polymers 22-30 LOC100508689 Homo sapiens 16-21 17356062-6 2007 AFM analysis of mucin polymers at the single molecule level provides new information about the genetic origins of individual polymers and the contributions of glycosylation to the physicochemical properties of mucins, which can be correlated with information obtained from biochemistry, antibody binding assays, and molecular biology techniques. Polymers 125-133 LOC100508689 Homo sapiens 16-21 16213127-6 2006 The bioadhesion potential was governed by the polymer ability to interact with mucin/agar (highest for carrageenan, Carbopol, xanthan gum and NaCMC). Polymers 46-53 LOC100508689 Homo sapiens 79-84 10496665-3 1999 This approach is applied to study the interaction of gastric porcine mucin with three viscosity grades of a mucoadhesive polymer, sodium carboxymethylcellulose. Polymers 121-128 LOC100508689 Homo sapiens 69-74 11231115-1 2001 The aim of the present work was to investigate the influence of polymer concentration and polymer:mucin weight ratio on chitosan--mucin interaction, assessed by means of viscosimetric measurements. Polymers 64-71 LOC100508689 Homo sapiens 130-135 11231115-8 2001 The results obtained suggest that two different types of rheological interaction occur between chitosan and mucin in both media, depending on polymer concentration and polymer:mucin weight ratio: one is characterized by a minimum in viscosity and occurs at higher polymer:mucin weight ratio, the other one produces a positive rheological synergism and is observed in presence of an excess of mucin. Polymers 142-149 LOC100508689 Homo sapiens 108-113 10496665-4 1999 RESULTS: By comparing the compliance models of polymer solutions and their mixtures with mucin, prepared at different concentrations and concentration ratios, we observed an increase in the order of the model of the mixtures at the lowest polymer concentration for all the three viscosity grades; this effect is more pronounced for the low viscosity grade. Polymers 47-54 LOC100508689 Homo sapiens 89-94 10496665-4 1999 RESULTS: By comparing the compliance models of polymer solutions and their mixtures with mucin, prepared at different concentrations and concentration ratios, we observed an increase in the order of the model of the mixtures at the lowest polymer concentration for all the three viscosity grades; this effect is more pronounced for the low viscosity grade. Polymers 239-246 LOC100508689 Homo sapiens 89-94 10027213-8 1999 The two polymers investigated showed different rheological interaction properties with mucin. Polymers 8-16 LOC100508689 Homo sapiens 87-92 1892323-2 1991 Mucin condensation and its decondensation upon exocytosis can be explained by the theory of polymer gel phase transition. Polymers 92-99 LOC100508689 Homo sapiens 0-5 1694990-0 1990 A simple rheological method for the in vitro assessment of mucin-polymer bioadhesive bond strength. Polymers 65-72 LOC100508689 Homo sapiens 59-64 1694990-1 1990 A simple viscometric method was used to quantify mucin-polymer bioadhesive bond strength. Polymers 55-62 LOC100508689 Homo sapiens 49-54 34056092-0 2021 Stereochemical Control Yields Mucin Mimetic Polymers. Polymers 44-52 LOC100508689 Homo sapiens 30-35 2261512-3 1990 Because the mucin polymer network is held together by tangles and low energy bonds, the rheological properties of this gel are mainly determined by the degree of postexocytotic hydration. Polymers 18-25 LOC100508689 Homo sapiens 12-17 2261516-0 1990 Wettability of polymers by mucin aqueous solutions. Polymers 15-23 LOC100508689 Homo sapiens 27-32 2261516-4 1990 The wettabilities of the polymers by mucin aqueous solutions have been studied as a function of protein concentration and related to the surface tensions. Polymers 25-33 LOC100508689 Homo sapiens 37-42 2261516-7 1990 This adhesion tension behavior appeared to be in agreement with previous data we have published concerning the quantity and state of mucin which are adsorbed to polymers characterized by different surface properties. Polymers 161-169 LOC100508689 Homo sapiens 133-138 6591994-4 1984 Application of the methods is illustrated with data on the size distribution of a tracheal mucin glycoprotein solution as an example of a polydisperse polymer solution of biorheological interest. Polymers 151-158 LOC100508689 Homo sapiens 91-96 34418212-7 2021 The mixing ratio of linear polymers versus crosslinker and the length of the linear polymer were varied, thus delivering a library of compositionally defined mucin-inspired constructs. Polymers 27-35 LOC100508689 Homo sapiens 158-163 34418212-7 2021 The mixing ratio of linear polymers versus crosslinker and the length of the linear polymer were varied, thus delivering a library of compositionally defined mucin-inspired constructs. Polymers 84-91 LOC100508689 Homo sapiens 158-163 35450630-4 2022 The polymer exhibited superior mucoadhesive capability compared to carboxymethyl cellulose through the interaction between maleimide moiety and mucin. Polymers 4-11 LOC100508689 Homo sapiens 144-149 3502764-10 1987 The data show that extracellular Ca++, in concentrations similar to those found in the mucus of cystic fibrosis patients (2 to 4 mM) can produce a four-fold decrease in the diffusivity of the newly released mucin polymer network, resulting in a slow rate of swelling, and a mucus that remains thick for long periods of time. Polymers 213-220 LOC100508689 Homo sapiens 207-212 33601537-1 2021 Mucin polymers in the tear film protect the corneal surface from pathogens and modulate the tear-film flow characteristics. Polymers 6-14 LOC100508689 Homo sapiens 0-5 33183638-7 2021 Moreover, the polymer exhibited strong binding ability with mucin. Polymers 14-21 LOC100508689 Homo sapiens 60-65 32270438-2 2020 In this paper, we describe experimental correlation of real-time properties of a polymer with pendant drug molecules, with predicted values obtained from studying in silico molecular interactions of this polymer with ocular surface proteins (mucin) for formulating an ophthalmic in situ gel. Polymers 81-88 LOC100508689 Homo sapiens 242-247 32270438-7 2020 The studies further reveal that molecular interactions of MUC-1 with the drug in the drug-polymer conjugate influence the binding orientation of the drug-polymer to mucin. Polymers 90-97 LOC100508689 Homo sapiens 165-170 31105217-8 2019 Also, the properties of complexes composed of CS and mucin vary as a function of the sources and preparation of the polymers. Polymers 116-124 LOC100508689 Homo sapiens 53-58 31362433-5 2019 Quartz microbalance with dissipation and neutron reflectometry measurements on thin mucin layers deposited on silica supports highlighted the occurrence of polymer interaction with mucin on the molecular scale. Polymers 156-163 LOC100508689 Homo sapiens 84-89 31362433-5 2019 Quartz microbalance with dissipation and neutron reflectometry measurements on thin mucin layers deposited on silica supports highlighted the occurrence of polymer interaction with mucin on the molecular scale. Polymers 156-163 LOC100508689 Homo sapiens 181-186 32435858-9 2020 From these results, it was suggested that by increasing the viscosity of the nanoemulsion, there was high affinity between the added polymer and mucin, and sustained drug release was useful for enhancing the bioavailability of the polymer-containing nanoemulsions. Polymers 133-140 LOC100508689 Homo sapiens 145-150 32435858-9 2020 From these results, it was suggested that by increasing the viscosity of the nanoemulsion, there was high affinity between the added polymer and mucin, and sustained drug release was useful for enhancing the bioavailability of the polymer-containing nanoemulsions. Polymers 231-238 LOC100508689 Homo sapiens 145-150 31493509-8 2019 This study demonstrates that the properties of NPs made of organic drug molecules can be modified by the addition of polymers, which may impact on their interaction with mucin and therefore on their potential systemic absorption. Polymers 117-125 LOC100508689 Homo sapiens 170-175 30424240-9 2018 Interestingly, the deposition of single mucin layers (mucin/water)3 has also been proven, however, the capsules were unstable, most probably due to additional (to hydrogen bonding) electrostatic interactions in the case of the two polymers used. Polymers 231-239 LOC100508689 Homo sapiens 40-45 29729636-3 2018 Among the various methods reported in the literature for the evaluation of the mucoadhesive properties of polymers, in the early 1990s, the study of the rheological variation of the polymer solutions after mixing with a mucin solution/dispersion has been proposed as an approach to measure the strength of the mucoadhesive joint. Polymers 106-114 LOC100508689 Homo sapiens 220-225 30424240-9 2018 Interestingly, the deposition of single mucin layers (mucin/water)3 has also been proven, however, the capsules were unstable, most probably due to additional (to hydrogen bonding) electrostatic interactions in the case of the two polymers used. Polymers 231-239 LOC100508689 Homo sapiens 54-59 28117832-2 2017 The primary structural components of mucus are mucin glycoproteins, which crosslink to form a complex polymer network that surrounds microbes. Polymers 102-109 LOC100508689 Homo sapiens 47-52 27809639-0 2018 Polymer coated liposomes for use in the oral cavity - a study of the in vitro toxicity, effect on cell permeability and interaction with mucin. Polymers 0-7 LOC100508689 Homo sapiens 137-142 28088003-9 2017 Acetylcysteine-stabilized polymers exhibited an optimum cross-linked structure, with free thiol groups ensuring polymer-mucin interactions, resulting in the best mucoadhesive properties. Polymers 26-34 LOC100508689 Homo sapiens 120-125 28081602-3 2017 In this work, polymer-based protein engineering was used to examine the role of polymer physicochemical properties on the activity and stability of the chymotrypsin-polymer conjugates and their degree of binding to intestinal mucin. Polymers 14-21 LOC100508689 Homo sapiens 226-231 28081602-3 2017 In this work, polymer-based protein engineering was used to examine the role of polymer physicochemical properties on the activity and stability of the chymotrypsin-polymer conjugates and their degree of binding to intestinal mucin. Polymers 80-87 LOC100508689 Homo sapiens 226-231 28081602-3 2017 In this work, polymer-based protein engineering was used to examine the role of polymer physicochemical properties on the activity and stability of the chymotrypsin-polymer conjugates and their degree of binding to intestinal mucin. Polymers 80-87 LOC100508689 Homo sapiens 226-231 28081602-5 2017 The influence of polymer charge on chymotrypsin-polymer conjugate mucin binding, bioactivity, and stability in stomach acid was determined. Polymers 17-24 LOC100508689 Homo sapiens 66-71 28081602-5 2017 The influence of polymer charge on chymotrypsin-polymer conjugate mucin binding, bioactivity, and stability in stomach acid was determined. Polymers 48-55 LOC100508689 Homo sapiens 66-71 28081602-6 2017 Cationic polymers covalently attached to chymotrypsin showed high mucin binding, while zwitterionic, uncharged, and anionic polymers showed no mucin binding. Polymers 9-17 LOC100508689 Homo sapiens 66-71 30979166-7 2016 Through this review, the prospective potential of polymer based analogs to serve as mucin mimic is suggested. Polymers 50-57 LOC100508689 Homo sapiens 84-89 26964399-3 2015 These polymers are able to form covalent bonds (disulphide linkages) with the mucin glycoproteins. Polymers 6-14 LOC100508689 Homo sapiens 78-83 26418812-5 2016 In addition, the deposition of a dense polymer coating on the mucin network was shown to act as a barrier to control diffusion and improved the structural stability under simulated oral chemical conditions. Polymers 39-46 LOC100508689 Homo sapiens 62-67 26272125-0 2015 Optimal design for studying mucoadhesive polymers interaction with gastric mucin using a quartz crystal microbalance with dissipation (QCM-D): Comparison of two different mucin origins. Polymers 41-49 LOC100508689 Homo sapiens 75-80 26272125-4 2015 QCM-D has shown its potential as a highly sensitive technique that provides information about the interaction of mucoadhesive polymers with gastric mucin. Polymers 126-134 LOC100508689 Homo sapiens 148-153 25818947-7 2015 Along with previously-established anti-inflammatory, anti-viral, and hydrocarbon-solubilizing properties of mucin, the results of this study establish mucin as a readily-available, chemically-versatile, naturally-biocompatible alternative to complex multifunctional synthetic polymers as building blocks in the design of biomaterials for sustained drug delivery. Polymers 276-284 LOC100508689 Homo sapiens 151-156 25911164-4 2015 Several polymer related factors like molecular weight, chain length, degree of cross-linking, hydration, functional groups, charge, polymer concentration and several environmental and physiological factors like contact time, mucin turnover rate and mucus viscosity affect the degree of mucoadhesion. Polymers 8-15 LOC100508689 Homo sapiens 225-230 25041765-3 2014 Furthermore, we investigated the gelation of both types of mucin solutions in response to a reduction in pH, where we observed the formation of large-scale heterogeneities within the polymer solutions, typical of microphase-separated gels. Polymers 183-190 LOC100508689 Homo sapiens 59-64 22451922-1 2012 MUC2, the major colonic mucin, forms large polymers by N-terminal trimerization and C-terminal dimerization. Polymers 43-51 LOC100508689 Homo sapiens 24-29 23787748-4 2013 Architecturally and functionally diverse polymers are used to protect enzymes sterically from inactivation and to promote interactions with mucin on the stomach wall. Polymers 41-49 LOC100508689 Homo sapiens 140-145 23298059-1 2013 We introduce a comprehensive model of a mucin-like polyelectrolyte gel swelling-deswelling which includes the ion-mediated crosslinking of polymer strands and the exchange of divalent and monovalent ions in the gel. Polymers 139-146 LOC100508689 Homo sapiens 40-45 21918918-6 2011 It was found that the drug or polymers alone, as well as the various formulations, were more likely to adhere to mucin than to nasal tissue. Polymers 30-38 LOC100508689 Homo sapiens 113-118 21905030-5 2012 We validate our assay by applying it to mucin hydrogels and show that the permeability properties of these mucin hydrogels can be modulated by polymer density and pH, in agreement with previous results obtained from single particle tracking. Polymers 143-150 LOC100508689 Homo sapiens 40-45 21905030-5 2012 We validate our assay by applying it to mucin hydrogels and show that the permeability properties of these mucin hydrogels can be modulated by polymer density and pH, in agreement with previous results obtained from single particle tracking. Polymers 143-150 LOC100508689 Homo sapiens 107-112