Hydroxypropyl Guar−Borate Interactions with Tear Film Mucin and Lysozyme Journal Articles

abstract

• The interactions of hydroxypropyl guar (HPG) with boric acid, lysozyme, and mucin were characterized by rheology, light scattering, electrophoresis, and isothermal titration calorimetry to help understand how HPG interacts with tear film components. Borate binds to guar under pH, temperature, and ionic strength conditions representative of those found in the eye. The HPG-borate complexes behave as anionic polyelectrolytes and thus interact with cationic lysozyme, a major tear film protein, whereas HPG-borate does not appear to bind to mucin, an anionic glycoprotein. The interactions of HPG, borate, lysozyme, and mucin can be explained by two physical interactions: (1) pH-dependent binding of borate to carbohydrates and (2) the electrostatic attraction of oppositely charged macromolecules.

authors

• Lu, Chen
• Kostanski, Leopold
• Ketelson, Howard
• Meadows, David
• Pelton, Robert

status

• published 

publication date

• October 1, 2005

has subject area

• Animals (MeSH)
• Borates (MeSH)
• Cattle (MeSH)
• Chemical Physics (Science Metrix)
• Chickens (MeSH)
• Galactans (MeSH)
• Galactose (MeSH)
• Hydrogen-Ion Concentration (MeSH)
• Macromolecular Substances (MeSH)
• Mannans (MeSH)
• Mannose (MeSH)
• Mucins (MeSH)
• Muramidase (MeSH)
• Plant Gums (MeSH)
• Polysaccharides (MeSH)
• Protein Binding (MeSH)
• Scattering, Radiation (MeSH)
• Static Electricity (MeSH)

published in

• Langmuir  Journal

keywords

• Animals
• Borates
• Cattle
• Chickens
• Galactans
• Galactose
• Hydrogen-Ion Concentration
• Macromolecular Substances
• Mannans
• Mannose
• Mucins
• Muramidase
• Plant Gums
• Polysaccharides
• Protein Binding
• Scattering, Radiation
• Static Electricity

Digital Object Identifier (DOI)

• 10.1021/la050988g

PubMed ID

• 16229524

start page

• 10032

end page

• 10037

volume

• 21

issue

• 22