2017
DOI: 10.1142/s1793545816500437
|View full text |Cite
|
Sign up to set email alerts
|

Spectroscopic analysis of the interaction between tetra-(p-sulfoazophenyl-4-aminosulfonyl)-substituted aluminum (III) phthalocyanines and serum albumins

Abstract: The binding interaction between tetra-(p-sulfoazophenyl-4-aminosulfonyl)-substituted aluminum (III) phthalocyanine (AlPc), and two-serum albumins (bovine serum albumin (BSA) and human serum albumin (HSA)) has been investigated. AlPc could quench the intrinsic°uorescence of BSA and HSA through a static quenching process. The primary and secondary binding sites of AlPc on BSA were domain I and III of BSA. The primary binding site of AlPc on HSA was domain I, and the secondary binding sites of AlPc on HSA were fo… Show more

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
3
1

Citation Types

1
3
0

Year Published

2019
2019
2022
2022

Publication Types

Select...
8

Relationship

0
8

Authors

Journals

citations
Cited by 9 publications
(4 citation statements)
references
References 30 publications
(36 reference statements)
1
3
0
Order By: Relevance
“…The interactions between other photosensitizers and HSA have been computed or experimentally determined in several studies [67][68][69]. In comparison with our results, Guevara et al study showed that three glycosylated photosensitizers bind to HSA close to Sudlow's site I and form strong interactions with TRP214 [67].…”
Section: Discussionsupporting
confidence: 81%
See 1 more Smart Citation
“…The interactions between other photosensitizers and HSA have been computed or experimentally determined in several studies [67][68][69]. In comparison with our results, Guevara et al study showed that three glycosylated photosensitizers bind to HSA close to Sudlow's site I and form strong interactions with TRP214 [67].…”
Section: Discussionsupporting
confidence: 81%
“…Zheng et al predicted the interaction of tetra-(p-sulfoazophenyl-4-aminosulfonyl)-substituted aluminium(III) phthalocyanine photosensitizer with HSA. Their study also showed that the photosensitizer interacts with TRP214 AA residue [68]. Szafraniec's study showed that two derivatives of chlorophyll bind to HAS to Sudlow's sites I and II [69].…”
Section: Discussionmentioning
confidence: 97%
“…Albumins, despite relatively low isoelectric point of approximately 4.7, are well-known to strongly bind the acidic drugs mainly into the positively charged binding sites formed prevalently by basic amino acid residues (Lys, Arg, and His). 28 The binding of anionic Pcs to albumins is also well known in the literature, 24,25,29 but reports on the interaction of cationic Pcs with this protein have also been reported. 25,26 However, in line with our previous observations, 12 no qualitative changes in the absorption and emission spectra or Φ F values were observed upon the addition of BSA into a PBS solution of hydrophilic cationic Pcs 4−6, indicating no detectable interaction with this protein (Figures S6, S7).…”
Section: ■ Resultsmentioning
confidence: 95%
“…On this sense, aluminum phthalocyanines exhibit a high affinity binding site constant (K ~ 3–4 × 10 7 L mol −1 ) that includes a strong binding site and other weaker sites 44 . For instance, substituted aluminum (III) phthalocyanines interact with domains I and III in bovine serum albumin as the primary and secondary binding sites, respectively 45 . Taking into consideration these high affinity interactions, the design of phthalocyanine–albumin assemblies as novel nanosystems has been explored 46 .…”
Section: Discussionmentioning
confidence: 99%