2009
DOI: 10.1016/j.colsurfb.2008.12.016
|View full text |Cite
|
Sign up to set email alerts
|

Kinetic study on the binding of lectin to mannose residues in a polymer brush

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
2
2
1

Citation Types

1
23
1

Year Published

2010
2010
2017
2017

Publication Types

Select...
6
3

Relationship

1
8

Authors

Journals

citations
Cited by 33 publications
(25 citation statements)
references
References 63 publications
1
23
1
Order By: Relevance
“…We have found that K d for the mannosides and Con A interactions are in the nanomolar range and are slightly smaller than previously reported values for mannose–Con A interaction using SPR ( K d =135–400 nM) [47] and QCM ( K d = 250–400 nM) techniques [48, 49]. It has also been found that binding affinity of multivalent ligands to lectins are stronger compared to monovalent ligands [50, 51].…”
Section: Resultscontrasting
confidence: 51%
“…We have found that K d for the mannosides and Con A interactions are in the nanomolar range and are slightly smaller than previously reported values for mannose–Con A interaction using SPR ( K d =135–400 nM) [47] and QCM ( K d = 250–400 nM) techniques [48, 49]. It has also been found that binding affinity of multivalent ligands to lectins are stronger compared to monovalent ligands [50, 51].…”
Section: Resultscontrasting
confidence: 51%
“…50,51,53 Values of k on = 2.0 × 10 4 M −1 s −1 and k off = 2.6 × 10 −3 s −1 corresponding to K d = 130 nM were reported for Con A interacting with SAMs of a thiolated PEG linker terminated in a mannose unit on 5 nm Au islands. 53 As noted by Bellapadrona et al, a range of values of k off between 2.48 × 10 −4 s −1 and 1.2 × 10 −2 s −1 , and of k on ranging from 5.2 × 10 3 M −1 s −1 to 1.4 × 10 5 M −1 s −1 , corresponding to K d values ranging from 42 nM to 423 nM have been reported for the Con A–mannose interaction depending upon measurement method, details of surface modification, and experimental conditions.…”
Section: Resultsmentioning
confidence: 99%
“…Au nanoparticles supported on glass have been modified by polymer brushes with many pendant glucose residues and LSPR was used to determine a binding constant from real-time analysis of 5.0 ± 0.2 × 10 5 M −1 noted as larger than that for Con A binding to methyl α-D-glucopyranoside of 2.4 ± 0.1 × 10 3 M −1 in solution and attributed to multipoint binding effects. 50 The use of supported gold nanoparticles modified with a polymer brush having pendant mannose units was applied to follow Con A binding, 51 resulting in an apparent association constant determined from analysis of real-time association kinetics data of 7.4 ± 0.1 × 10 6 M −1 , noted as much greater than that for Con A tomethyl α-D-mannopyranoside in solution of 7.6 ± 0.2 × 10 3 M −1 , with the difference attributed to multipoint binding effects. Au nanoparticles bound to glass modified by 3-aminopropyltrimethoxysilane were modified by dodecanethiol SAMs into which a N -acetylglucosamine glycolipid was inserted, and shift in the LSPR peak wavelength due to Con A binding was observed in transmission mode in real-time for both association and dissociation.…”
Section: Introductionmentioning
confidence: 99%
“…Interestingly, the membrane could be regenerated upon acid treatment ("acid leaching method") without any degradation. Kitano et al [128,134] reported the synthesis of thiol-terminated glycopolymers (Entry 100 and 116; Table 2) and their grafting on a colloidal gold-immobilized glass substrate for the study of binding and adsorption processes by UV-Vis spectrophotometer with the help of a localized surface plasmon resonance. To this end, 2-(2-bromoisobutyroyloxy)ethyl disulfide A34 was used to initiated the polymerization of glucoside methacrylate M34a and mannoside methacrylate derivatives with M n = 1800-8600 Da).…”
Section: Scheme 14mentioning
confidence: 99%