ArticleBiomacromolecules2007
Polyamine analogues bind human serum albumin.
Article in Biomacromolecules, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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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.
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Who cites it
19 citing papers in PubMed, 188 citations in OpenAlex.
- Human Serum Albumin Affinity for Putrescine Using ITC and STD-NMR.International journal of molecular sciences · 2025Article
- Insights into the binding of buspirone to human serum albumin using multi-spectroscopic and molecular docking techniques.Heliyon · 2024Article
- Spectroscopic Analysis of the Effect of Ibuprofen Degradation Products on the Interaction between Ibuprofen and Human Serum Albumin.Current protein & peptide science · 2024Article
- Bone-Targeting Nanoparticles of a Dendritic (Aspartic acid)International journal of molecular sciences · 2022Article
- Non-toxic Polymeric Dots with the Strong Protein-Driven Enhancement of One- and Two-Photon Excited Emission for Sensitive and Non-destructive Albumin Sensing.ACS applied materials & interfaces · 2022Article
- Spectroscopic and molecular docking studies for characterizing binding mechanism and conformational changes of human serum albumin upon interaction with Telmisartan.Saudi pharmaceutical journal : SPJ : the official publication of the Saudi Pharmaceutical Society · 2020Article
- Antidepressant drug-protein interactions studied by spectroscopic methods based on fluorescent carbon quantum dots.Heliyon · 2019Article
- A Chalcone-Based Potential Therapeutic Small Molecule That Binds to Subdomain IIA in HSA Precisely Controls the Rotamerization of Trp-214.ACS omega · 2018Article
- Hematological Effects of Gold Nanorods on Erythrocytes: Hemolysis and Hemoglobin Conformational and Functional Changes.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2017Article
- Article
- Spectroscopic Study on the Interaction between Naphthalimide-Polyamine Conjugates and Bovine Serum Albumin (BSA).Molecules (Basel, Switzerland) · 2015Article
- Non-covalent binding analysis of sulfamethoxazole to human serum albumin: Fluorescence spectroscopy, UV-vis, FT-IR, voltammetric and molecular modeling.Journal of pharmaceutical analysis · 2015Article
- Screening and characterisation of antimicrobial properties of semisynthetic betulin derivatives.PloS one · 2014Article
- New insight into molecular interaction of heavy metal pollutant--cadmium(II) with human serum albumin.Environmental science and pollution research international · 2014Article
- Molecular dynamics simulation studies of betulinic acid with human serum albumin.Journal of molecular modeling · 2012Article
- Probing the binding sites of antibiotic drugs doxorubicin and N-(trifluoroacetyl) doxorubicin with human and bovine serum albumins.PloS one · 2012Article
- Article
- Biogenic and synthetic polyamines bind bovine serum albumin.Biomacromolecules · 2010Article
- Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Polyamine analogues show antitumor activity in experimental models, and their ability to alter activity of cytotoxic chemotherapeutic agents in breast cancer is well documented. Association of polyamines with nucleic acids and protein is included in their mechanism of action. The aim of this study was to examine the interaction of human serum albumin (HSA) with several polyamine analogues, such as 1,11-diamino-4,8-diazaundecane (333), 3,7,11,15-tetrazaheptadecane.4HCl (BE-333), and 3,7,11,15,19-pentazahenicosane.5HCl (BE-3333), in aqueous solution at physiological conditions using a constant protein concentration and various polyamine contents (microM to mM). FTIR, UV-visible, and CD spectroscopic methods were used to determine the polyamine binding mode and the effects of polyamine complexation on protein stability and secondary structure. Structural analysis showed that polyamines bind nonspecifically (H-bonding) via polypeptide polar groups with binding constants of K333 = 9.30 x 10(3) M(-1), KBE-333 = 5.63 x 10(2) M(-1), and KBE-3333 = 3.66 x 10(2) M(-1). The protein secondary structure showed major alterations with a reduction of alpha-helix from 55% (free protein) to 43-50% and an increase of beta-sheet from 17% (free protein) to 29-36% in the 333, BE-333, and BE-3333 complexes, indicating partial protein unfolding upon polyamine interaction. HSA structure was less perturbed by polyamine analogues compared to those of the biogenic polyamines.
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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.