Abstract
Surface plasmon resonance (SPR) spectroscopy was applied for the first time to study online the association of the blood-brain barrier proteins ZO-1 (zona occludens protein 1) and occludin. The GuK motif of ZO-1 (amino acids 644-812) was identified as the sequence domain that bound to the cytosolic, C-terminal tail of occludin (amino acids 378-521). The nitric oxide (·NO) liberator SIN-1 (3-morpholinosydnonimine) reduced the binding affinity of ZO-1 to occludin, indicating a direct effect of ·NO and NO-related species on the tight junction proteins sealing the blood-brain barrier. We propose that SPR spectroscopy is a novel approach for investigating the interactions of tight junction proteins directly and continuously for pharmacological studies.
Original language | English |
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Title of host publication | Blood-Spinal Cord and Brain Barriers in Health and Disease |
Publisher | Elsevier |
Pages | 11-17 |
Number of pages | 7 |
ISBN (Electronic) | 9780080528229 |
ISBN (Print) | 9780126390117 |
DOIs | |
Publication status | Published - Jan 1 2004 |
Keywords
- NO, SIN-1
- Occludin
- Protein interaction
- SPR
- Tight junctions
- ZO-1
ASJC Scopus subject areas
- Medicine(all)
- Neuroscience(all)