ArticleInternational journal of biological macromolecules2019
Novel combinations of experimental and computational analysis tested on the binding of metalloprotoporphyrins to albumin.
Article in International journal of biological macromolecules, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 26 citations in OpenAlex.
- Organic-solvent mediated self-assembly of protoporphyrin IX with human serum albumin.International journal of biological macromolecules · 2025Article
- Identification of Blood Transport Proteins to Carry Temoporfin: A Domino Approach from Virtual Screening to Synthesis and In Vitro PDT Testing.Pharmaceutics · 2023Article
- Multi-wavelength analytical ultracentrifugation of biopolymer mixtures and interactions.Analytical biochemistry · 2022Review
- Zinc binding strength of proteins dominants zinc uptake in Caco-2 cells.RSC advances · 2022Article
- A 200 nanoseconds all-atom simulation of the pH-dependent EF loop transition in bovine β-lactoglobulin. The role of the orientation of the E89 side chain.Journal of biomolecular structure & dynamics · 2022Article
- A calibration disk for the correction of radial errors from chromatic aberration and rotor stretch in the Optima AUC™ analytical ultracentrifuge.European biophysics journal : EBJ · 2020Article
- Moving analytical ultracentrifugation software to a good manufacturing practices (GMP) environment.PLoS computational biology · 2020Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
The evidence that Human Serum Albumin (HSA) binds metal ions and organometallic compounds has generated interest in its physiological role as a metalloprotein and as a vehicle for synthetic biology applications (e.g., synthetic blood and solar energy conversion). HSA has been shown to bind metallo-porphyrins, however, the structural details of such interactions are available only for the HSA:heme complex. A typical challenge for studying the interaction of proteins with metalloporphyrins is the poor solubility of the ligands that affect the characterization the complexes. The manuscript shows that a combination of dialysis and centrifugation yields aqueous solutions that contain >90% HSA:porphyrin complexes and virtually eliminate aggregated ligands. The removal of aggregates increases the quality of the optical spectroscopy data which, in turn, yield more accurate binding constants (~0.1 and 2.1 × 10
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Registered trials
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