2013
DOI: 10.1016/j.jpba.2012.10.008
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Application of Bio-Layer Interferometry for the analysis of protein/liposome interactions

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Cited by 70 publications
(55 citation statements)
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“…3b), indicating strong binding affinity between protein and telodendrimer. However, the dissociation rate was too slow in PBS and not sufficient for dissociation constant ( k off ) fitting[52]. BSA, the most abundant protein in blood plasma, was observed to accelerate telodendrimer dissociation in a concentration dependent manner (Fig.…”
Section: Resultsmentioning
confidence: 99%
“…3b), indicating strong binding affinity between protein and telodendrimer. However, the dissociation rate was too slow in PBS and not sufficient for dissociation constant ( k off ) fitting[52]. BSA, the most abundant protein in blood plasma, was observed to accelerate telodendrimer dissociation in a concentration dependent manner (Fig.…”
Section: Resultsmentioning
confidence: 99%
“…The binding kinetics were measured on the basis of the attachment of liposomes that increase the thickness of the layer of protein-coated surface that is correlated directly to the spectral shift as measured by biolayer interferometry. 420 This method has considerable high-throughput capability for identification of lead biomolecular drugs. Similarly, viral interactions with receptors on host cell membranes can be mimicked using receptor-bound liposomes.…”
Section: Analytical Applicationsmentioning
confidence: 99%
“…Using BLI the affinity and kinetics of various interactions can be determined, such as protein-protein, 52 protein-nucleic acid 53 or binding of proteins to liposomes. 54 …”
Section: Bio-layer Interferometrymentioning
confidence: 99%