Binding of pyrene-1-butyric acid to serum albumin: Species differences.

Matsushita, Yasuo; Moriguchi, Ikuo

doi:10.1248/bpb1978.12.762

Cited by 3 publications

(4 citation statements)

References 19 publications

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“…Pyrene probes have strong absorption bands in the UV region, a high fluorescence quantum yield and long life time of the excited singlet state (can be examined with a nanosecond flash photolysis system). However, the literature concerning binding of pyrene and its derivatives to HSA or other serum albumins is not extensive [13,[19][20][21][22][23][24][25]. The albumin-induced changes of absorption and fluorescence spectra have been reported, but in most cases the authors do not specify unambiguously the probe/protein binding sites.…”

Section: Introductionmentioning

confidence: 99%

Interaction of 1-pyrene sulfonic acid sodium salt with human serum albumin

Steblecka

Wolszczak

Szajdzińska‐Piętek

2016

Journal of Luminescence

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Section: Introductionmentioning

confidence: 99%

Interaction of 1-pyrene sulfonic acid sodium salt with human serum albumin

Steblecka

Wolszczak

Szajdzińska‐Piętek

2016

Journal of Luminescence

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“…To test the above strategy, we chose the pyrene chromophore to serve as the donor and coumarin chromophore as the acceptor, and tested the ability of bovine serum albumin (BSA) to form the ternary complex. This choice of chromophores and the host is based on the reports that several pyrene-derivatives such as pyrene-1-butyric acid (PBA, Chart 1), 6 amides of PBA made from numerous amino acids, 7 and amino acid derivatives of 1(1-amino)methylpyrene 8 bind to BSA with moderate to high affinities. In a similar manner, several coumarin derivatives such as warfarin, 9 coumarin 540A (C540A) 10 are known to bind to BSA with moderate to high binding constants.…”

Section: Introductionmentioning

confidence: 99%

Towards building artificial light harvesting complexes: enhanced singlet-singlet energy transfer between donor and acceptor pairs bound to albumins

Kumar

Duff

2008

Photochem Photobiol Sci

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Specific donor and acceptor pairs have been assembled in bovine serum albumin (BSA), at neutral pH and room temperature, and these dye-protein complexes indicated efficient donor to acceptor singlet-singlet energy transfer. For example, pyrene-1-butyric acid served as the donor and Coumarin 540A served as the acceptor. Both the donor and the acceptor bind to BSA with affinity constants in excess of 2x10(5) M(-1), as measured in absorption and circular dichroism (CD) spectral titrations. Simultaneous binding of both the donor and the acceptor chromophores was supported by CD spectra and one chromophore did not displace the other from the protein host, even when limited concentrations of the host were used. For example, a 1:1:1 complex between the donor, acceptor and the host can be readily formed, and spectral data clearly show that the binding sites are mutually exclusive. The ternary complexes (two different ligands bound to the same protein molecule) provided opportunities to examine singlet-singlet energy transfer between the protein-bound chromophores. Donor emission was quenched by the addition of the acceptor, in the presence of limited amounts of BSA, while no energy transfer was observed in the absence of the protein host, under the same conditions. The excitation spectra of the donor-acceptor-host complexes clearly show the sensitization of acceptor emission by the donor. Protein denaturation, as induced by the addition of urea or increasing the temperature to 360 K, inhibited energy transfer, which indicate that protein structure plays an important role. Sensitization also proceeded at low temperature (77 K) and diffusion of the donor or the acceptor is not required for energy transfer. Stern-Volmer quenching plots show that the quenching constant is (3.1+/-0.2)x10(4) M(-1), at low acceptor concentrations (<35 microM). Other albumins such as human and porcine proteins also served as good hosts for the above experiments. For the first time, non-natural systems have been self-assembled which can capture donor-acceptor pairs and facilitate singlet-singlet energy transfer. Such systems may form a basis for the design and construction of protein-based multi-chromophore self-assemblies for solar light harvesting, conversion and storage.

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“…Further, due to their excellent binding properties, these globular proteins are used as functional product in various biomedical processes. For protein binding studies, bovine serum albumin (BSA) has universally been used as a model owing to its close resemblance with human serum albumin, abundance, and cost effectiveness. − So far, to the best of our knowledge, mainly small molecule pyrene derivatives with high hydrophobicity have been used for the binding study with DNA and BSA. − , However, Haldar et. al have reported interactions of pyrene-tagged polyethylene glycol with BSA and human serum albumin (HSA) by steady state fluorescence studies .…”

Section: Introductionmentioning

confidence: 99%

“…19−25 So far, to the best of our knowledge, mainly small molecule pyrene derivatives with high hydrophobicity have been used for the binding study with DNA and BSA. [19][20][21][22]26 However, Haldar et. al have reported interactions of pyrene-tagged polyethylene glycol with BSA and human serum albumin (HSA) by steady state fluorescence studies.…”

Section: Introductionmentioning

confidence: 99%

Study of the Fluorescence Based Applications of Pyrene-Tagged Poly(N-vinyl-2-pyrrolidone)

Mitra

Singh

Hira

et al. 2016

ACS Biomater. Sci. Eng.

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In this study we have explored the fluorescence based applications of luminescent pyrene-tagged PNVP (PyPNVP) reported in our previous work (Int. J. Polym. Mater. Polym. Biomater.201665269276). PyPNVP has successfully acted as “turn off” chemosensor for metal ions Cu2+, Hg2+, and Pb2+. It has also successfully acted as a fluorescent probe for critical micellar concentration (CMC) determination of amphiphilic block copolymer of poly(d,l-lactide) and poly(N-vinylpyrrolidone) (PDLLA42 -b-PNVP120) (M n = 19 400 g/mol and PD = 1.52). It has also successfully shown an interaction with both plasmid and calf thymus (CT) deoxyribonucleic acids (DNAs) as evidenced by its fluorescence quenching. A different magnitude and type of quenching has been observed for both the cases which may be useful in distinguishing different kinds of DNAs. In order to further understand the potential of PyPNVP in various biotechnological processes, its binding property with bovine serum albumin (BSA) has also been studied. The efficient quenching of intrinsic fluorescence of BSA by PyPNVP through binding and the occurrence of the fluorescence resonance energy transfer (FRET) type of interaction have been studied using steady state, synchronous, and 3D fluorescence spectroscopies. Moreover, a fluorescence microscopic cell imaging study has revealed the significant uptake of PyPNVP in the nucleus of HEPG2 and U87 cells compared to free Py. In addition, the cytotoxicity study showed the tolerance of PyPNVP in all the cell lines tested with no significant cytotoxicity at lower concentrations.

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Binding of pyrene-1-butyric acid to serum albumin: Species differences.

Cited by 3 publications

References 19 publications

Interaction of 1-pyrene sulfonic acid sodium salt with human serum albumin

Interaction of 1-pyrene sulfonic acid sodium salt with human serum albumin

Towards building artificial light harvesting complexes: enhanced singlet-singlet energy transfer between donor and acceptor pairs bound to albumins

Study of the Fluorescence Based Applications of Pyrene-Tagged Poly(N-vinyl-2-pyrrolidone)

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