ArticleThe protein journal2013
Interaction of human serum albumin with novel 3,9-disubstituted perylenes.
Article in The protein journal, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
4 citing papers in PubMed, 16 citations in OpenAlex.
- Organic-solvent mediated self-assembly of protoporphyrin IX with human serum albumin.International journal of biological macromolecules · 2025Article
- Effects of Visible-Light Irradiation of Protoporphyrin IX on the Self-Assembly of Tubulin Heterodimers.Chemphyschem : a European journal of chemical physics and physical chemistry · 2016Article
- Biophysical characterization of the interaction of human albumin with an anionic porphyrin.Biochemistry and biophysics reports · 2016Article
- Characterization of novel perylene diimides containing aromatic amino acid side chains.Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Human serum albumin (HSA) has been used as a model for the binding of a number of different ligands, including polyaromatic hydrocarbons, to proteins. In this case we have investigated the interaction of HSA with a novel set of perylene derivatives. Di-substituted perylene analogues have been synthesized as potentially useful organic photovoltaic materials. Their photophysical properties may make them viable for fuel cell applications too. However, these molecules are poorly soluble especially in aqueous solvents. Binding to water-soluble proteins may provide a way to solubilize them. At the same time one can study whether the photophysical processes initiated by the irradiation of a perylene ligand can cause conformational changes to the host protein. With the present study we demonstrated that of the three perylene derivatives investigated only one, the dimethoxy analogue, has a significant affinity for HSA at a binding site near the bottom of the central cleft (in proximity of the Trp214 residue). The small affinity prevents any significant photoinduced changes to occur in the protein.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.