Does fluorescence of ANS reflect its binding to PAMAM dendrimer?
The analysis of binding between dendrimer and ANS has shown that (1) fluorescence reflects binding of probe to dendrimer, (2) parameters of binding are K b ∼ 0.75 × 10 5 M −1 and n ∼ 0.5. The analysis of binding between cationic PAMAM G5 dendrimer and anionic fluorescent probe using fluorescence and...
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Published in: | Bioorganic chemistry Vol. 35; no. 2; pp. 170 - 174 |
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Main Authors: | , , |
Format: | Journal Article |
Language: | English |
Published: |
United States
Elsevier Inc
01-04-2007
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Subjects: | |
Online Access: | Get full text |
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Summary: | The analysis of binding between dendrimer and ANS has shown that (1) fluorescence reflects binding of probe to dendrimer, (2) parameters of binding are
K
b
∼
0.75
×
10
5
M
−1 and
n
∼
0.5.
The analysis of binding between cationic PAMAM G5 dendrimer and anionic fluorescent probe using fluorescence and equilibrium dialysis has been made. It was found that at low concentrations of ANS the double fluorimetric titration technique can be successfully used for quantitative analysis of binding of ANS to dendrimer. Based on fluorescence and dialysis data the constants of binding and the number of binding centers were calculated for binding of ANS to PAMAM G5 dendrimer:
K
b is approx. (0.5–1)
×
10
5
M
−1 and
n is (0.5–0.7). |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0045-2068 1090-2120 |
DOI: | 10.1016/j.bioorg.2006.10.003 |