Understanding the adsorption and potential tear film stability properties of recombinant human lubricin and bovine submaxillary mucins in an in vitro tear film model
Journal Article
·
· Colloids and Surfaces. B, Biointerfaces
- Stanford Univ., CA (United States)
- Nagaoka Univ. of Technology (Japan)
- Novartis Pharma AG, Basel (Switzerland)
The wetting and adsorption properties for two glycoproteins, recombinant human lubricin and bovine submaxillary mucins (BSM) were evaluated on hydrophilic and hydrophobic glass dome surfaces in a simplified in vitro tear film model. Herein, we show that both recombinant human lubricin (rh-lubricin) and BSM solutions render surfaces hydrophilic and when the fluid films reach 500 nm or less, the fluids resist evaporation-driven breakup through a volumetric flux across the surface, which we believe is due to evaporation-driven solutocapillary flows. rh-Lubricin was able to maintain a wet film without spontaneous breakup for longer periods of time than BSM at lower concentrations, which we attribute to differences in adsorption properties, measured by QCM-D, that result from surface charge and structural differences (confirmed by zeta potential, DLS, and SAXS measurements).
- Research Organization:
- SLAC National Accelerator Laboratory (SLAC), Menlo Park, CA (United States)
- Sponsoring Organization:
- National Institutes of Health (NIH); National Science Foundation (NSF); USDOE; USDOE Office of Science (SC), Basic Energy Sciences (BES)
- Grant/Contract Number:
- AC02-76SF00515
- OSTI ID:
- 1769032
- Alternate ID(s):
- OSTI ID: 1778402
- Journal Information:
- Colloids and Surfaces. B, Biointerfaces, Journal Name: Colloids and Surfaces. B, Biointerfaces Vol. 195; ISSN 0927-7765
- Publisher:
- ElsevierCopyright Statement
- Country of Publication:
- United States
- Language:
- English
Single bubble and drop techniques for characterizing foams and emulsions
|
journal | December 2020 |
Similar Records
Cell-free translation of messenger RNA from bovine submaxillary glands and identification of the apomucin
A novel approach for chemically deglycosylating O-linked glycoproteins. The deglycosylation of submaxillary and respiratory mucins
Structure and dynamics of porcine submaxillary mucin as determined by natural abundance carbon-13 NMR spectroscopy
Conference
·
Thu May 01 00:00:00 EDT 1986
· Fed. Proc., Fed. Am. Soc. Exp. Biol.; (United States)
·
OSTI ID:7108758
A novel approach for chemically deglycosylating O-linked glycoproteins. The deglycosylation of submaxillary and respiratory mucins
Journal Article
·
Mon Jan 27 23:00:00 EST 1992
· Biochemistry; (United States)
·
OSTI ID:5618329
Structure and dynamics of porcine submaxillary mucin as determined by natural abundance carbon-13 NMR spectroscopy
Journal Article
·
Tue Jul 28 00:00:00 EDT 1987
· Biochemistry; (United States)
·
OSTI ID:5941094