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Mucin structure, aggregation, physiological functions and biomedical applications

Journal

CURRENT OPINION IN COLLOID & INTERFACE SCIENCE
Volume 11, Issue 2-3, Pages 164-170

Publisher

ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.cocis.2005.11.001

Keywords

mucin; aggregation; gelation; gastric mucus; mucoadhesion; glycoprotein; biorheology

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An understanding of the basic structure, viscoelastic properties and interactions of mucin glycoproteins is of considerable interest to food science because of the important protective role that these macromolecules play in gastric physiology. The polymeric/colloidal behavior of mucins is complicated due to their large size (2-50 MDa) and complex structure with domains involving hydrophilic/hydrophobic, hydrogen bonds and electrostatic interactions, and their propensity to aggregate and form complexes with other polymers. These properties are also of direct relevance to the numerous diseases involving mucins, and to the problems of uptake of nutrients and delivering drugs through the mucus barrier. In this review we describe the current state of understanding of the relevant properties, with an emphasis on recent research. The findings described in this review are of direct relevance to the uptake of nutrients in digestion. (C) 2005 Published by Elsevier Ltd.

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