Cited by 160

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Interaction Between Chitosan and Mucin: Fundamentals and Applications

Collado-González, Mar, González Espinosa, Yadira, Goycoolea, Francisco M.·2019·Biomimetics

Abstract

The term chitosan (CS) refers to a family of aminopolysaccharides derived from chitin. Among other properties, CS is nontoxic, mucoadhesive and can be used for load and transport drugs. Given these and other physicochemical and biological properties, CS is an optimal biopolymer for the development of transmucosal drug delivery systems, as well as for the treatment of pathologies related to mucosal dysfunctions. Mucins are glycoprotein macromolecules that are the major components of mucus overlaying epithelia. CS interacts with mucin and adsorbs on and changes the rheology of mucus. However, CS and mucins denote families of polymers/macromolecules with highly variable chemical structure, properties, and behavior. To date, their interactions at the molecular level have not been completely unraveled. Also, the properties of complexes composed of CS and mucin vary as a function of the sources and preparation of the polymers. As a consequence, the mucoadhesion and drug delivery properties of such complexes vary as well. The breadth of this review is on the molecular interactions between CS and mucin. In particular, in vitro and ex vivo characterization methods to investigate both the interactions at play during the formation of CS-mucin complexes, and the advances on the use of CS for transmucosal drug delivery are addressed.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.3390/biomimetics4020032

Cites

1 of 1 references verified0 citation errors · 0 not checkable

Statistics

Figures

Figure 1 Structure of the mucus gel on the epithelial surfaces. Reprinted from [1], with permission from Elsevier.
Figure 1 Structure of the mucus gel on the epithelial surfaces. Reprinted from [1], with permission from Elsevier.CC BY · PubMed Central
Figure 2 The domain structure of mucins. VWD: Von Wiellebrand D-domain, C8: conserved cysteine rich domain, TIL: trypsin inhibitor-like cystein-rich domain, CysD: domain rich in cystein residues, VWC: Von Wiellebrand C-domain, PTS: PTS domains, CK: cystein knot domain, NIDO: nidogen homology region, AMOP: the adhesion-associated domain in MUC4 and other proteins, SEA: sea-urchin sperm protein, enterokinase, and agrin domain, TM: transmembrane domain. Reprinted with permission from Springer Nature, Copyright 2016 [2].
Figure 2 The domain structure of mucins. VWD: Von Wiellebrand D-domain, C8: conserved cysteine rich domain, TIL: trypsin inhibitor-like cystein-rich domain, CysD: domain rich in cystein residues, VWC: Von Wiellebrand C-domain, PTS: PTS domains, CK: cystein knot domain, NIDO: nidogen homology region, AMOP: the adhesion-associated domain in MUC4 and other proteins, SEA: sea-urchin sperm protein, enterokinase, and agrin domain, TM: transmembrane domain. Reprinted with permission from Springer Nature, Copyright 2016 [2].CC BY · PubMed Central
Figure 3 Representation of the crosslinking of mucins. Extracted with permission from [1].
Figure 3 Representation of the crosslinking of mucins. Extracted with permission from [1].CC BY · PubMed Central
Figure 4 Structure of fully N-acetylated chitin (a), fully N-deacetylated chitosan (b) and representative partially N-acetylated chitosan sequence (c).
Figure 4 Structure of fully N-acetylated chitin (a), fully N-deacetylated chitosan (b) and representative partially N-acetylated chitosan sequence (c).CC BY · PubMed Central
Figure 5 Possible scenarios in the interaction of chitosan-based nanosystems and mucins. Once the nanosystems achieve the mucus, they can go through the mucus and reach the epithelium (a), be shed with the mucus (b) or get trapped in the mucus gel (c).
Figure 5 Possible scenarios in the interaction of chitosan-based nanosystems and mucins. Once the nanosystems achieve the mucus, they can go through the mucus and reach the epithelium (a), be shed with the mucus (b) or get trapped in the mucus gel (c).CC BY · PubMed Central
Figure 6 Intrinsic and extrinsic features that alter the interactions between chitosan and mucin.
Figure 6 Intrinsic and extrinsic features that alter the interactions between chitosan and mucin.CC BY · PubMed Central

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Show all 1 references

Research works printed but not linked: 66

  1. Cone, 2009, Barrier properties of mucus, Adv. Drug Deliv. Rev., 61, 75, 10.1016/j.addr.2008.09.008 · DOI
  2. Johansson, 2016, Immunological aspects of intestinal mucus and mucins, Nat. Rev. Immunol., 16, 639, 10.1038/nri.2016.88 · DOI · Paper page
  3. Bansil, 2018, The biology of mucus: Composition, synthesis and organization, Adv. Drug Deliv. Rev., 124, 3, 10.1016/j.addr.2017.09.023 · DOI
  4. Johansson, 2011, The two mucus layers of colon are organized by the MUC2 mucin, whereas the outer layer is a legislator of host-microbial interactions, Proc. Natl. Acad. Sci. USA, 108, 4659, 10.1073/pnas.1006451107 · DOI
  5. Forstner, 1978, Intestinal mucins in health and disease, Digestion, 17, 234, 10.1159/000198115 · DOI
  6. Corfield, 1992, Mucin degradation in the human colon: Production of sialidase, sialate O-acetylesterase, N-acetylneuraminate lyase, arylesterase, and glycosulfatase activities by strains of fecal bacterial, Infect. Immun., 60, 3971, 10.1128/iai.60.10.3971-3978.1992 · DOI
  7. Lee, 2005, Porcine gastric mucin (PGM) at the water/poly(dimethylsiloxane) (PDMS) interface: Influence of pH and ionic strength on its conformation, adsorption, and aqueous lubrication properties, Langmuir, 21, 8344, 10.1021/la050779w · DOI · Paper page
  8. Nordman, 1997, Mucus glycoproteins from pig gastric mucosa: Identification of different mucin populations from the surface epithelium, Biochem. J., 326, 903, 10.1042/bj3260903 · DOI
  9. Celli, 2007, Rheology of gastric mucin exhibits a pH-dependent sol-gel transition, Biomacromolecules, 8, 1580, 10.1021/bm0609691 · DOI
  10. Silva, 2012, Interaction of chitosan and mucin in a biomembrane model environment, J. Colloid Interface Sci., 376, 289, 10.1016/j.jcis.2012.03.027 · DOI
  11. Derrien, 2010, Mucin-bacterial interactions in the human oral cavity and digestive tract, Gut Microbes, 1, 254, 10.4161/gmic.1.4.12778 · DOI · Paper page
  12. Nikogeorgos, 2015, “Bio-glues” to enhance slipperiness of mucins: Improved lubricity and wear resistance of porcine gastric mucin (PGM) layers assisted by mucoadhesion with chitosan, Soft Matter, 11, 489, 10.1039/C4SM02021A · DOI
  13. Geyer, 2006, Strategies for analysis of glycoprotein glycosylation, Biochim. Biophys. Acta, 1764, 1853, 10.1016/j.bbapap.2006.10.007 · DOI
  14. Deplancke, 2001, Microbial modulation of innate defense: Globet cells and the intestinal mucus layer, Am. J. Clin. Nutr., 73, 1131S, 10.1093/ajcn/73.6.1131S · DOI · Paper page
  15. Karlsson, 1997, Glycosilation differences between pig gastric mucin populations: A comparative study of the neutral oligosaccharides using mass spectrometry, Biochem. J., 326, 911, 10.1042/bj3260911 · DOI
  16. Gunning, 2013, Mining the “glycocode”–exploring the spatial distribution of glycans in gastrointestinal mucin using force spectroscopy, FASEB J. Off. Publ. Fed. Am. Soc. Exp. Biol., 27, 2342
  17. Thomsson, 1999, Liquid chromatography-electrospray mass spectrometry as a tool for the analysis of sulfated oligosaccharides from mucin glycoproteins, J. Chromatogr. A, 854, 131, 10.1016/S0021-9673(99)00625-1 · DOI
  18. Svensson, 2010, Mucin layers and multilayers—Physicochemical properties and applications, Curr. Opin. Colloid Interface Sci., 15, 395, 10.1016/j.cocis.2010.05.015 · DOI
  19. Turner, 1999, Cysteine-rich regions of pig gastric mucin contain von Wiellebrand factor and cystine knot domains at the carboxyl terminal, Biochim. Biophys. Acta, 1447, 77, 10.1016/S0167-4781(99)00099-8 · DOI
  20. Yakubov, 2007, Molecular structure and rheological properties of short-side-chain heavily glycosylated porcine stomach mucin, Biomacromolecules, 8, 3467, 10.1021/bm700607w · DOI
  21. Menchicchi, 2014, Structure of chitosan determines its interactions with mucin, Biomacromolecules, 15, 3550, 10.1021/bm5007954 · DOI
  22. Mushi, 2016, Nanostructurally Controlled Hydrogel Based on Small-Diameter Native Chitin Nanofibers: Preparation, Structure, and Properties, ChemSusChem, 9, 989, 10.1002/cssc.201501697 · DOI
  23. Kurita, 2006, Chitin and chitosan: Functional biopolymers from marine crustaceans, Mar. Biotechnol., 8, 203, 10.1007/s10126-005-0097-5 · DOI
  24. Rinaudo, 2006, Non-covalent interactions in polysaccharide systems, Macromol. Biosci., 6, 590, 10.1002/mabi.200600053 · DOI
  25. Silva, 2017, Ionic liquids in the processing and chemical modification of chitin and chitosan for biomedical applications, Green Chem., 19, 1208, 10.1039/C6GC02827F · DOI
  26. Kadokawa, J.-i. (2016). Dissolution, gelation, functionalization, and material preparation of chitin using ionic liquids. Pure Appl. Chem., 88. · DOI
  27. Lamarque, 2007, Thermodynamic aspects of the heterogeneous deacetylation of β-chitin: Reaction mechanisms, Biomacromolecules, 8, 1942, 10.1021/bm070021m · DOI
  28. Jang, 2004, Physicochemical characterization of α-chitin, β-chitin, and γ-chitin separated from natural resources, J. Polym. Sci. Part A Polym. Chem., 42, 3423, 10.1002/pola.20176 · DOI
  29. Leiva, 2015, Improving the performance of chitosan in the synthesis and stabilization of gold nanoparticles, Eur. Polym. J., 68, 419, 10.1016/j.eurpolymj.2015.04.032 · DOI
  30. Thakur, 2014, Recent Advances in Graft Copolymerization and Applications of Chitosan: A Review, ACS Sustain. Chem. Eng., 2, 2637, 10.1021/sc500634p · DOI
  31. Rinaudo, 2006, Chitin and chitosan: Properties and applications, Prog. Polym. Sci., 31, 603, 10.1016/j.progpolymsci.2006.06.001 · DOI
  32. Lee, 2004, Physicochemical properties and blood compatibility of acylated chitosan nanoparticles, Carbohydr. Polym., 58, 371, 10.1016/j.carbpol.2004.06.033 · DOI
  33. Philippova, 2012, Aggregation of some water-soluble derivatives of chitin in aqueous solutions: Role of the degree of acetylation and effect of hydrogen bond breaker, Carbohydr. Polym., 87, 687, 10.1016/j.carbpol.2011.08.043 · DOI
  34. Panos, 2008, New Drug Delivery Systems Based on Chitosan, Curr. Drug Discov. Technol., 5, 333, 10.2174/157016308786733528 · DOI
  35. Aranaz, 2009, Functional characterization of chitin and chitosan, Curr. Chem. Biol., 3, 203
  36. Rinaudo, 1999, Influence of acetic acid concentration on the solubilization of chitosan, Polymers, 40, 7029, 10.1016/S0032-3861(99)00056-7 · DOI
  37. Boucard, 2007, Polyelectrolyte microstructure in chitosan aqueous and alcohol solutions, Biomacromolecules, 8, 1209, 10.1021/bm060911m · DOI
  38. Kasaai, 2007, Calculation of Mark–Houwink–Sakurada (MHS) equation viscometric constants for chitosan in any solvent–temperature system using experimental reported viscometric constants data, Carbohydr. Polym., 68, 477, 10.1016/j.carbpol.2006.11.006 · DOI
  39. Gartner, 2010, Medidas de la rigidez del quitosano en solución a través de la viscosidad intrínseca, Rev. Fac. Ing. Univ. Antioquía, 53, 20
  40. Morris, 2009, Macromolecular conformation of chitosan in dilute solution: A new global hydrodynamic approach, Carbohydr. Polym., 76, 616, 10.1016/j.carbpol.2008.11.025 · DOI
  41. Vauthier, 2008, Specific permeability modulation of intestinal paracellular pathway by chitosan-poly(isobutylcyanoacrylate) core-shell nanoparticles, Eur. J. Pharm. Biopharm. Off. J. Arb. Fur Pharm. Verfahr. E.V, 69, 436
  42. Canali, 2012, Chitosan enhances transcellular permeability in human and rat intestine epithelium, Eur. J. Pharm. Biopharm., 80, 418, 10.1016/j.ejpb.2011.11.007 · DOI
  43. Bhattarai, 2010, Chitosan-based hydrogels for controlled, localized drug delivery, Adv. Drug Deliv. Rev., 62, 83, 10.1016/j.addr.2009.07.019 · DOI
  44. Hsu, 2012, Elucidating the signaling mechanism of an epithelial tight-junction opening induced by chitosan, Biomaterials, 33, 6254, 10.1016/j.biomaterials.2012.05.013 · DOI
  45. Szymanska, 2015, Stability of chitosan—A challenge for pharmaceutical and biomedical applications, Mar. Drugs, 13, 1819, 10.3390/md13041819 · DOI
  46. Liu, 2018, A functional chitosan-based hydrogel as a wound dressing and drug delivery system in the treatment of wound healing, RSC Adv., 8, 7533, 10.1039/C7RA13510F · DOI
  47. Menchicchi, 2015, Biophysical analysis of the molecular interactions between polysaccharides and mucin, Biomacromolecules, 16, 924, 10.1021/bm501832y · DOI
  48. Mackie, 2017, Innovative Methods and Applications in Mucoadhesion Research, Macromol. Biosci., 17, 1600534, 10.1002/mabi.201600534 · DOI
  49. Morariu, 2012, The Behavior of Chitosan in Solvents with Different Ionic Strengths, Ind. Eng. Chem. Res., 51, 12959, 10.1021/ie301309g · DOI
  50. Villora, 2017, Chitosan as stabilizing agent for negatively charged nanoparticles, Carbohydr. Polym., 161, 63, 10.1016/j.carbpol.2016.12.043 · DOI
  51. Wagner, 2017, A Rheological Study of the Association and Dynamics of MUC5AC Gels, Biomacromolecules, 18, 3654, 10.1021/acs.biomac.7b00809 · DOI
  52. Sander, 2014, A mechanistic based approach for enhancing buccal mucoadhesion of chitosan, Int. J. Pharm., 461, 280, 10.1016/j.ijpharm.2013.10.047 · DOI
  53. Dedinaite, 2005, Mucin-chitosan complexes at the solid-liquid interface: Multilayer formation and stability in surfactant solutions, Langmuir, 21, 9502, 10.1021/la0511844 · DOI
  54. Haugstad, 2015, Direct determination of chitosan-mucin interactions using a single-molecule strategy: Comparison to alginate-mucin interactions, Polymers, 7, 161, 10.3390/polym7020161 · DOI
  55. Li, 2010, A novel method for modifying AFM probe to investigate the interaction between biomaterial polymers (chitosan-coated PLGA) and mucin film, Eur. J. Pharm. Biopharm., 75, 277, 10.1016/j.ejpb.2010.02.013 · DOI
  56. Feng, 2015, Surface charge effect on mucoadhesion of chitosan based nanogels for local anti-colorectal cancer drug delivery, Colloids Surf. B Biointerfaces, 128, 439, 10.1016/j.colsurfb.2015.02.042 · DOI
  57. Xu, 2017, Mucoadhesive chitosan hydrogels as rectal drug delivery vessels to treat ulcerative colitis, Acta Biomater., 48, 247, 10.1016/j.actbio.2016.10.026 · DOI
  58. Deacon, 2000, Atomic force microscopy of gastric mucin and chitosan mucoadhesive systems, Biochem. J., 348, 557, 10.1042/bj3480557 · DOI
  59. Rossi, 2000, Characterization of chitosan hydrocloride-mucin interaction by means of viscosimetric and turbidimetric measurements, Eur. J. Pharm. Sci., 10, 251, 10.1016/S0928-0987(00)00065-8 · DOI
  60. Rossi, 2001, Characterization of chitosan hydrochloride-mucin rheological interaction: Influence of polymer concentration and polymer:mucin weight ratio, Eur. J. Pharm. Sci., 12, 479, 10.1016/S0928-0987(00)00194-9 · DOI
  61. Kootala, 2018, Reinforcing Mucus Barrier Properties with Low Molar Mass Chitosans, Biomacromolecules, 19, 872, 10.1021/acs.biomac.7b01670 · DOI
  62. Szymanska, 2014, Vaginal chitosan tablets with clotrimazole-design and evaluation of mucoadhesive properties using porcine vaginal mucosa, mucin and gelatine, Chem. Pharm. Bull., 62, 160, 10.1248/cpb.c13-00689 · DOI
  63. Diop, 2015, Design, characterisation, and bioefficiency of insulin-chitosan nanoparticles after stabilisation by freeze-drying or cross-linking, Int. J. Pharm., 491, 402, 10.1016/j.ijpharm.2015.05.065 · DOI
  64. Dhawan, 2004, Evaluation of mucoadhesive properties of chitosan microspheres prepared by different methods, AAPS PharmSciTech, 5, 1, 10.1208/pt050467 · DOI
  65. Zhang, 2018, Design and intestinal mucus penetration mechanism of core-shell nanocomplex, J. Control. Release Off. J. Control. Release Soc., 272, 29, 10.1016/j.jconrel.2017.12.034 · DOI
  66. Hattori, 2017, Characterization of a water-soluble chitosan derivative and its potential for submucosal injection in endoscopic techniques, Carbohydr. Polym., 175, 592, 10.1016/j.carbpol.2017.08.028 · DOI

Cited by

Sorted by citations

Metadata

Authors
Collado-González, M., González Espinosa, Y., & Goycoolea, F. M.
Venue
Biomimetics
Publisher
MDPI AG
Published
2019-04-25
Volume
4
Issue
2
Pages
32
ISSN
2313-7673
Cited by
160
References
1
Language
en

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review