Interactive Association of Drugs Binding to Human Serum Albumin

Drug Delivery Systems: Entering the Mainstream

Allen, T. M., & Cullis, P. R. (2004) · Science · doi:10.1126/science.1095833 · Cited by 4,552

Atomic structure and chemistry of human serum albumin

He, X. M., & Carter, D. C. (1992) · Nature · doi:10.1038/358209a0 · Cited by 3,833

An inhibitor of Bcl-2 family proteins induces regression of solid tumours

Oltersdorf, T., Elmore, S. W., Shoemaker, A. R., Armstrong, R. C., Augeri, D. J., Belli, B., Bruncko, M., Deckwerth, T. L., Dinges, J., Hajduk, P. J., et al. (2005) · Nature · doi:10.1038/nature03579 · Cited by 3,407

Structure of Serum Albumin

Carter, D. C., & Ho, J. X. (1994) · Advances in protein chemistry · doi:10.1016/s0065-3233(08)60640-3 · Cited by 3,184

All About Albumin: Biochemistry, Genetics, and Medical Applications

Peters, T. (1995) · Thammasat University Digital Collections · Cited by 3,089

Albumin as a drug carrier: Design of prodrugs, drug conjugates and nanoparticles

Kratz, F. (2008) · Journal of Controlled Release · doi:10.1016/j.jconrel.2008.05.010 · Cited by 2,151

Human serum albumin: From bench to bedside

Fanali, G., di Masi, A., Trezza, V., Marino, M., Fasano, M., & Ascenzi, P. (2011) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2011.12.002 · Cited by 2,008

Structural Basis of the Drug-binding Specificity of Human Serum Albumin

Ghuman, J., Zunszain, P. A., Petitpas, I., Bhattacharya, A. A., Otagiri, M., & Curry, S. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.07.075 · Cited by 1,941

Crystal structure of human serum albumin at 2.5 Å resolution

Sugio, S., Kashima, A., Mochizuki, S., Noda, M., & Kobayashi, K. (1999) · Protein Engineering Design and Selection · doi:10.1093/protein/12.6.439 · Cited by 1,816

The Characterization of Two Specific Drug Binding Sites on Human Serum Albumin

Sudlow, G., Birkett, D. J., & WADE, D. N. (1975) · Molecular Pharmacology · doi:10.1016/s0026-895x(25)10691-3 · Cited by 1,769

Polymeric nanotherapeutics: An emerging therapeutic approach for the management of neurodegenerative disorders

Chakraborty, P., Bhattacharyya, C., Sahu, R., Dua, T. K., Kandimalla, R. J. L., & Dewanjee, S. (2023) · Journal of Drug Delivery Science and Technology · doi:10.1016/j.jddst.2023.105267 · Cited by 12

Application of Fisetin to the Quantitation of Serum Albumin

Park, J. M., Do, V., Seo, Y., Duong, M. T. H., Ahn, H.-C., Huh, H. J., & Lee, M. (2020) · Journal of Clinical Medicine · doi:10.3390/jcm9020459 · Cited by 11

Binding Kinetics of Ruthenium Pyrithione Chemotherapeutic Candidates to Human Serum Proteins Studied by HPLC-ICP-MS

Marković, K., Milačić, R., Marković, S., Kladnik, J., Turel, I., & Ščančar, J. (2020) · Molecules · doi:10.3390/molecules25071512 · Cited by 11

An albumin-binding Gd-HPDO3A contrast agent for improved intravascular retention

Tear, L. R., Carrera, C., Dhakan, C. B., Cavallari, E., Travagin, F., Calcagno, C., Aime, S., & Gianolio, E. (2021) · Inorganic Chemistry Frontiers · doi:10.1039/d1qi00128k · Cited by 11

Serum albumin acted as an effective carrier to improve the stability of bioactive flavonoid

Yang, Y.-D., Lu, N., & Tian, R. (2023) · Amino Acids · doi:10.1007/s00726-023-03347-5 · Cited by 10

Physiological changes in the albumin-bound non-esterified free fatty acids critically influence heme/bilirubin binding properties of the protein: A comparative, in vitro, spectroscopic study using the endogenous biomolecules

Amoorahim, M., Ashrafi-Kooshk, M. R., Esmaeili, S., Shahlaei, M., Moradi, S., & Khodarahmi‬, R. (2020) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2020.118298 · Cited by 10

Deciphering the interactions of substituted chromones possessing acetylcholinesterase inhibition activity in human serum albumin matrix

Rohman, M. A., Baruah, P., Bhatta, A., & Mitra, S. (2019) · Journal of Molecular Liquids · doi:10.1016/j.molliq.2019.111210 · Cited by 10

Exploring the structure of a ruthenium acetate cluster for biological purposes

da Silva, C. F. N., Ramos, L. C. B., Rohrabaugh, T. N., Vandevord, J. M., da Silva, R. S., Turró, C., & Nikolaou, S. (2020) · Inorganic Chemistry Communications · doi:10.1016/j.inoche.2020.107810 · Cited by 10

Nanocarriers in the Delivery of Hydroxychloroquine to the Respiratory System: An Alternative to COVID-19

Cavalcanti, I. D. L., Macêdo, D. C. D. S., Macêdo, D. C. D. S., Cavalcanti, I. M. F., & Nogueira, M. C. D. B. L. (2020) · Current Drug Delivery · doi:10.2174/1567201817666200827110445 · Cited by 10

Beneficial Effects of Carvacrol on In Vitro Models of Metabolically-Associated Liver Steatosis and Endothelial Dysfunction: A Role for Fatty Acids in Interfering with Carvacrol Binding to Serum Albumin

Khalil, M., Serale, N., Diab, F., Baldini, F., Portincasa, P., Lupidi, G., & Vergani, L. (2022) · Current Medicinal Chemistry · doi:10.2174/0929867329666220401103643 · Cited by 10

The Formation of β-Cyclodextrin Complexes with Levofloxacin and Ceftriaxone as an Approach to the Regulation of Drugs’ Pharmacokinetic

Yakupova, L. R., Kopnova, T. Y., Скуредина, А. А., Le‐Deygen, I. M., Shustrov, P. N., Novoselov, A. M., & Kudryashova, E. V. (2023) · Colloid Journal · doi:10.1134/s1061933x22600488 · Cited by 10

Interaction of ANS with human serum albumin under confinement: Important insights and relevance

Malik, A., Kundu, J., Karmakar, S., Lai, S., & Chowdhury, P. K. (2015) · Journal of Luminescence · doi:10.1016/j.jlumin.2015.06.034 · Cited by 10

Characterization of the complex between native and reduced bovine serum albumin with aquacobalamin and evidence of dual tetrapyrrole binding

Dereven’kov, I. А., Hannibal, L., Makarov, S. V., Makarova, A. S., Molodtsov, P. A., & Koifman, O. I. (2018) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-018-1562-8 · Cited by 10

Spectroscopic Characterization of the Interaction between Dopamine and Human Serum Albumin

Khalid, I. M., Abusharkh, S. E., Samamarh, H., Alfaqeeh, R., Abuteir, M. M., & Darwish, S. M. (2019) · Open Journal of Biophysics · doi:10.4236/ojbiphy.2019.92009 · Cited by 9

The Molecular Recognition of Lurasidone by Human Serum Albumin: A Combined Experimental and Computational Approach

Živković, N., Mrkalić, E., Jelić, R., Tomović, J., Serafinović, M. Ć., Odović, J., & Sovrlić, M. (2025) · Molecules · doi:10.3390/molecules30071420 · Cited by 9

An insight into in silico strategies used for exploration of medicinal utility and toxicology of nanomaterials

Khan, T. (2025) · Computational Biology and Chemistry · doi:10.1016/j.compbiolchem.2025.108435 · Cited by 9

Europium probe binding to serum albumin and α 1 -AGP, key importance of configuration, charge and size complementarity

Li, H., Ng, L. W., Black, D. J., Han, W., Pál, R., & Parker, D. (2025) · Chemical Science · doi:10.1039/d5sc03017j · Cited by 9

Comparative binding studies of bacosine with human serum albumin and α-1-acid glycoprotein biophysical evaluation and computational approach

Yeggoni, D. P., Rachamallu, A., & Subramanyam, R. (2021) · Journal of Pharmaceutical and Biomedical Analysis · doi:10.1016/j.jpba.2021.114478 · Cited by 9

Elucidating the cellular uptake mechanisms of heptamethine cyanine dye analogues for their use as an anticancer drug‐carrier molecule for the treatment of glioblastoma

Cooper, E., Choi, P. J., Hwang, K., Nam, K. M., Kim, C., Shaban, T., Schweder, P. M., Mee, E. T., Correia, J. A., Turner, C. P., et al. (2022) · Chemical Biology & Drug Design · doi:10.1111/cbdd.14171 · Cited by 9

Molecular Ballet: Investigating the Complex Interaction between Self-Assembling Dendrimers and Human Serum Albumin via Computational and Experimental Methods

Cavalieri, G., Marson, D., Giurgevich, N., Valeri, R., Felluga, F., Laurini, E., & Pricl, S. (2024) · Pharmaceutics · doi:10.3390/pharmaceutics16040533 · Cited by 9

Co-Existing Nanoplastics Further Exacerbates the Effects of Triclosan on the Physiological Functions of Human Serum Albumin

Bao, Y., Wang, Y., Liu, H., Lan, J., Li, Z., Zong, W., & Zhao, Z. (2025) · Life · doi:10.3390/life15010112 · Cited by 9

A Short Review on the Delivery of Breast Anticancer Drug Tamoxifen and its Metabolites by Serum Proteins

Tajmir Riahi, H. A. (2016) · Journal of Nanomedicine Research · doi:10.15406/jnmr.2016.04.00080 · Cited by 9

Albumin micro/nanoparticles entrapping liposomes for itraconazole green formulation

Valle, M. J. D. J., Maderuelo, C., Castañeda, A. Z., & Navarro, A. S. (2017) · European Journal of Pharmaceutical Sciences · doi:10.1016/j.ejps.2017.05.066 · Cited by 9

Investigations of the molecular mechanism of diltiazem binding to human serum albumin in the presence of metal ions, glucose and urea

Farsad, S. A., Haghaei, H., Shaban, M., Zakariazadeh, M., & Soltani, S. (2021) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2021.1891137 · Cited by 9

Nafamostat Mesylate in Combination with the Mouse Amino-Terminal Fragment of Urokinase–Human Serum Albumin Improves the Treatment Outcome of Triple-Negative Breast Cancer Therapy

Zhou, Y., Yu, S., Chen, D., Li, H., Xu, P., Yuan, C., Jiang, L., & Huang, M. (2022) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.2c00297 · Cited by 8

Platelet-targeted thromboprophylaxis with a human serum albumin fusion drug: Preventing thrombosis and reducing cardiac ischemia/reperfusion injurywithout bleeding complications

Song, Y., Bienvenu, L. A., Bongcaron, V., Prijaya, S. A., Maluenda, A. C., Walsh, A. P. G., McFayden, J. D., Pietersz, G. A., Peter, K., & Wang, X. (2024) · Theranostics · doi:10.7150/thno.97517 · Cited by 8

Binding interaction of four azo linked copper (II) complexes with Human Serum Albumin (HSA): Spectroscopic and molecular docking explorations

Tripathi, M., Chauhan, S., Princess, R., Khan, R. H., Siddiqi, M. K., Syed, R., Kalam, M. A., Guha, S., & Sarkar, A. (2024) · Results in Chemistry · doi:10.1016/j.rechem.2024.101637 · Cited by 8

Synthesis and structural studies of 16‐ferrocenemethyl‐estra‐1,3,5(10)‐triene‐3,17β‐diol and its interaction with human serum albumin by fluorescence spectroscopy and in silico docking approaches

Carmona‐Negrón, J. A., Liboy-Lugo, J., Santana, A., & Meléndez, E. (2020) · Applied Organometallic Chemistry · doi:10.1002/aoc.5483 · Cited by 8

Recreational drugs 25I-NBOH and 25I-NBOMe bind to both Sudlow's sites I and II of human serum albumin (HSA): biophysical and molecular modeling studies

de Barros, W. A., Silva, M. D. M., Dantas, M. D. D. A., Santos, J. C. C., Figueiredo, Í. M., Chaves, O. A., Sant’Anna, C. M. R., & de Fátima, Â. (2021) · New Journal of Chemistry · doi:10.1039/d1nj00806d · Cited by 8

Tracking TRYCAT: A Critical Appraisal of Kynurenine Pathway Quantifications in Blood

Coppens, V., Verkerk, R. M., & Morrens, M. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.825948 · Cited by 9

The Role of Blood-Derived Factors in Protection and Regeneration of Aged Tissues

Höving, A. L., Schmidt, K. E., Kaltschmidt, B., Kaltschmidt, C., & Knabbe, C. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23179626 · Cited by 8

Discovery of tight-binding competitive inhibitors of dipeptidyl peptidase IV

Alonso, I. P., Valiente, P. A., Valdés‐Tresanco, M. E., Sánchez, Y. A., García, F. A., Díaz, L., García, G., Guirola, O., Pastor, D., Bergado, G., et al. (2021) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2021.12.056 · Cited by 8

Quantitative Morphometric, Physiological, and Metabolic Characteristics of Chickens and Mallards for Physiologically Based Kinetic Model Development

Scanes, C. G., Witt, J., Ebeling, M., Schaller, S., Baier, V., Bone, A. J., Preuß, T. G., & Heckmann, D. (2022) · Frontiers in Physiology · doi:10.3389/fphys.2022.858283 · Cited by 8

In Vitro and Ex Vivo Biocompatibility, Biomolecular Interactions, and Characterization of Graphene Quantum Dots and Its Glutathione-Modified Variant for Qualitative Cell Imaging

Peñafiel, M. J. P., Gutierrez-Beleño, L. M., Mendoza, C. D., Freire-Júnior, F. L., Lima, M. A., Teixeira, T., Rocha, F. V., Zolin, G. V. S., Garrido, S. S., Lazzarini, A. B., et al. (2025) · ACS Omega · doi:10.1021/acsomega.4c10014 · Cited by 7

Functionalized albumin nanoparticles: A multifunctional platform for enhanced brain drug delivery

Mohammad, H., Darwish, M., Katona, G., & Csóka, I. (2025) · Materials Today Bio · doi:10.1016/j.mtbio.2025.102616 · Cited by 7

Chiral 8-aminoBODIPY-based fluorescent probes with site selectivity for the quantitative detection of HSA in biological samples

Jithinraj, T. K., Saheer, V. C., & Chakkumkumarath, L. (2022) · The Analyst · doi:10.1039/d2an01525k · Cited by 7

Recent breakthroughs in innovative elements, multidimensional enhancements, derived technologies, and novel applications of PROTACs

Zhang, S.-H., Zeng, N., Xu, J., Liu, C., Xu, M., Sun, J., An, Y., Zhong, X., Miao, L.-T., Wang, S., et al. (2024) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2024.117584 · Cited by 9

Synthesis of Novel Benzothiazole–Profen Hybrid Amides as Potential NSAID Candidates

Ivanov, I., Manolov, S. P., Bojilov, D. G., Stremski, Y., Marc, G., Statkova‐Abeghe, S. M., Oniga, S. D., Oniga, O., & Nedialkov, P. T. (2024) · Molecules · doi:10.3390/molecules30010107 · Cited by 7

Neutrophil to albumin ratio predicts cardiovascular and all cause mortality in CVD patients with abnormal glucose metabolism

Li, J., Yang, M., Zhang, X., Huang, R., Zhang, Y., & Fan, K. (2025) · Scientific Reports · doi:10.1038/s41598-025-08130-y · Cited by 7

Physiological role of plasma and its components and the clinical implications of different methods of apheresis: A narrative review

Ahmadpoor, P., Aglaé, C., Cariou, S., Pambrun, E., Renaud, S., Garo, F., Darmon, R., Schultz, C., Prelipcean, C., Reboul, P., et al. (2020) · Therapeutic Apheresis and Dialysis · doi:10.1111/1744-9987.13567 · Cited by 7

Orthopalladated tetralone oxime compounds bearing tertiary phosphines: Synthesis, structure, biological and in silico studies

Velasques, J. M., de Souza, R. F. F., Silva, D. E. S., de Farias, R. L., Zanetti, R. D., Moreira, M. B., Ellena, J., Pereira, J. C. M., MAURO, A. E., de Oliveira, A. B., et al. (2021) · Journal of Organometallic Chemistry · doi:10.1016/j.jorganchem.2021.122184 · Cited by 7

Novel Post-translational Modifications in Human Serum Albumin

Kannan, S., Krishnankutty, R., & Souchelnytskyi, S. (2022) · Protein and Peptide Letters · doi:10.2174/0929866529666220318152509 · Cited by 7

Elucidation of the binding mechanism of astragaloside IV derivative with human serum albumin and its cardiotoxicity in zebrafish embryos

Wu, Y., Li, Z., Li, J.-Y., Zhou, Y., Wang, R., Chen, X.-Y., Qing, L., & Luo, P. (2022) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.987882 · Cited by 7

CaviDB: a database of cavities and their features in the structural and conformational space of proteins

Rueda, A. J. V., Bulgarelli, F. L., Palópoli, N., & Parisi, G. D. (2023) · Database · doi:10.1093/database/baad010 · Cited by 7

Biodistribution of Novel 68Ga-Radiolabelled HER2 Aptamers in Mice

Gijs, M., Becker, G., & Plenevaux, A. (2016) · Journal of Nuclear Medicine & Radiation Therapy · doi:10.4172/2155-9619.1000300 · Cited by 7

Molecular Structure-Affinity Relationship of Bufadienolides and Human Serum Albumin In Vitro and Molecular Docking Analysis

Zhou, J., Lu, G., Wang, H., Zhang, J., Duan, J., Ma, H., & Wu, Q. (2015) · PLoS ONE · doi:10.1371/journal.pone.0126669 · Cited by 7

Porous Reduced Graphene Oxide β-cyclodextrin Modified Electrode as Enhanced Sensing Platform for the Determination of Dihydrochalcone: Phloretin

Tandel, R. D., & Seetharamappa, J. (2018) · Journal of The Electrochemical Society · doi:10.1149/2.0611810jes · Cited by 7

Biomolecular study and conjugation of two para-aminobenzoic acid derivatives with serum proteins: drug binding efficacy and protein structural analysis

Chanphai, P., Cloutier, F., Oufqir, Y., Leclerc, M.-F., Eiján, A. M., Reyes‐Moreno, C., Bérubé, G., & Tajmir‐Riahi, H. A. (2020) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2020.1719889 · Cited by 7

Mass spectrometry methods and mathematical PK/PD model for decision tree-guided covalent drug development

Hossain, M. A., Brahme, R. R., Miller, B. C., Amin, J., de Barros, M., Schneider, J. L., Auclair, J. R., Mattos, C., Wang, Q., Agar, N. Y. R., et al. (2025) · Nature Communications · doi:10.1038/s41467-025-56985-6 · Cited by 6

Biomonitoring Xenobiotics in Human Biospecimens: Challenges, Advances, and the Future of Exposome Characterization

Zhu, X., Tang, X., Ng, C. A., Li, L., Lai, Y., Miller, G. W., Jiang, C., Barchowsky, A., Buchanich, J. M., & Gao, P. (2025) · Reviews of Environmental Contamination and Toxicology · doi:10.1007/s44169-025-00088-2 · Cited by 7

Novel fluorescent probe for human serum albumin detection and labeling: Biological applications and insights from molecular dynamics simulations

Li, X., Sang, R.-X., Zhang, J., Fan, J., Huang, F., Ding, B., Tian, Y. S., Xie, C., Ma, Y., & Xu, J. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.149294 · Cited by 6

Unusually High Affinity of the PLK Inhibitors RO3280 and GSK461364 to HSA and Its Possible Pharmacokinetic Implications

Fernández-Sainz, J., Pacheco-Liñán, P. J., Ripoll, C., González-Fuentes, J., Albaladejo, J., Bravo, I., & Garzón‐Ruiz, A. (2023) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.2c00849 · Cited by 6

Enzalutamide-human serum albumin interaction: Electrochemical exploration of complex formation and binding parameters

Chenguiti, F., Bakırhan, N. K., Gozelle, M., Doulache, M., Saïdat, B., Atıcı, E. B., & Özkan, S. A. (2024) · Microchemical Journal · doi:10.1016/j.microc.2024.110760 · Cited by 6

Elucidating the binding dynamics and structural impacts of Pt(II) and Pd(II) complexes on human serum albumin: A comprehensive spectroscopic and computational study

Mosavi, M., Divsalar, A., Karami, L., Rasouli, M., Moghadam, M. E., & Karizak, A. Z. (2024) · Journal of Molecular Liquids · doi:10.1016/j.molliq.2024.126055 · Cited by 6

Recent Updates on Interaction Studies and Drug Delivery of Antimalarials with Serum Albumin Proteins

Azeem, K., Irfan, I., Rashid, Q., Singh, S., Patel, R., & Abid, M. (2023) · Current Medicinal Chemistry · doi:10.2174/0929867330666230509121931 · Cited by 6

Bridging Soft Interaction and Excluded Volume in Crowded Milieu through Subtle Protein Dynamics

Majumdar, S., Rastogi, H., & Chowdhury, P. K. (2024) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.3c07266 · Cited by 6

Liposomal OTS964, a TOPK inhibitor: a simple method to estimate OTS964 association with liposomes that relies on enhanced OTS964 fluorescence when bound to albumin

Gilabert‐Oriol, R., Sutherland, B. W., Anantha, M., Pallaoro, A., & Bally, M. B. (2019) · Drug Delivery and Translational Research · doi:10.1007/s13346-019-00651-0 · Cited by 6

Underestimated Toxicity: UV Amplifies Low-Dose Cr(VI) Damage to Skin at Molecular and Tissue Levels

Jie, T., Hua, W., Lu, R., Lin, Y., Chen, X., Xu, K., Yu, H., Zhang, J., & Zheng, C. (2025) · Environmental Science & Technology · doi:10.1021/acs.est.5c07765 · Cited by 5

Protoporphyrin IX conjugated to piperazine or morpholine: Photophysical properties and photodynamic activity

Franco, M. D. S., Lapierre, T. J. W. J. D., Martinho, A. C. C., Bessas, N. C., Caetano, M. M., Tasso, T. T., Beletti, M. E., de Lima, R. G., Júnior, C. D. O. R., & Tsubone, T. M. (2025) · Dyes and Pigments · doi:10.1016/j.dyepig.2025.112649 · Cited by 5

Fluorene methoxycarbonyl-PEG-deferoxamine conjugates “hitchhike” with albumin in situ for iron overload therapy

Xu, L., Guan, R., Yu, B., Li, Y., Liu, H., & Jiang, Y. (2022) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2022.122136 · Cited by 5

Does Risk of Hyperhomocysteinemia Depend on Thiol-Disulfide Exchange Reactions of Albumin and Homocysteine?

Coppo, L., Scheggi, S., DeMontis, G., Priora, R., Frosali, S., Margaritis, A., Summa, D., Giuseppe, D. D., Ulivelli, M., & Simplicio, P. D. (2022) · Antioxidants and Redox Signaling · doi:10.1089/ars.2021.0269 · Cited by 5

Modification of the structural stability of human serum albumin in rheumatoid arthritis

Lin, H. L., Parkinson, D. H., Holman, J. C., Thompson, W. C., Anderson, C. N. K., Hadfield, M., Ames, S., Zuniga, N. R., Bowden, J. N., Quinn, C. F., et al. (2023) · PLoS ONE · doi:10.1371/journal.pone.0271008 · Cited by 5

Binding mechanism, photo-induced cleavage and computational studies of interaction cefepime drug with Human serum albumin

Al–Asbahy, W. M., Shamsi, M., Senan, A. M., & Al-Areqi, N. A. S. (2024) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2024.2304668 · Cited by 5

Molecular dynamics of structural effects of reactive carbonyl species derivate of lipid peroxidation on bovine serum albumin

Pineda-Alemán, R., Cabarcas-Herrera, C., Amador, A. A., Galindo‐Murillo, R., Pérez-González, H., Rodríguez-Cavallo, E., & Méndez-Cuadro, D. (2024) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2024.130613 · Cited by 5

Current analytical methods and applications used in the insight of serum proteins interactions with various food additives, pesticides, and contaminants

Erkmen, C., & Kabır, M. Z. (2024) · Exploration of Foods and Foodomics · doi:10.37349/eff.2024.00034 · Cited by 5

Computational study of antioxidant activity and bioavailability of papua red fruit (Pandanus conoideus Lam.) flavonoids through docking toward human serum albumin

Suprijono, M. M., Widjanarko, S. B., Sujuti, H., & Kurnia, D. (2019) · AIP conference proceedings · doi:10.1063/1.5109995 · Cited by 6

Mode of binding, kinetic and thermodynamic properties of a lipid-like drug (Fingolimod) interacting with Human Serum Albumin

Gholizadeh, S., Haghaei, H., Karami, H., Soltani, S., Zakariazadeh, M., & Shokri, J. (2022) · Bioimpacts · doi:10.34172/bi.2022.23383 · Cited by 5

Fabrication of branched polyethylenimin/alginic acid/poly(cyclohexane-1,4-diyl acetone dimethylene ketal as a nano size carrier for controlled release of 5-fluorouracil

Chen, P.-C., Yii, D., Tsai, H., Parasuraman, V. R., Prasannan, A., Kao, C., & Lai, J. (2019) · Reactive and Functional Polymers · doi:10.1016/j.reactfunctpolym.2019.03.006 · Cited by 5

Elucidating the binding mechanism of an antimigraine agent with a model protein: insights from molecular spectroscopic, calorimetric and computational approaches

Naik, R. S., & Seetharamappa, J. (2022) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2022.2053747 · Cited by 5

Structural and evolutionary analysis unveil functional adaptations in the promiscuous behavior of serum albumins

Rueda, A. J. V., Benítez, G. I., Sommese, L. M., Ardanaz, S. M., Borucki, E. L., Palópoli, N., Iglesias, L. E., & Parisi, G. D. (2022) · Biochimie · doi:10.1016/j.biochi.2022.02.004 · Cited by 5

Fast Determination of Protein Binding Constants and Sites to Active Flavonoids and Phenolic Acids by Affinity Capillary Electrophoresis and Fluorescence Spectroscopy

Zheng, P., Wang, X., Cui, Y., Tang, R., Yu, H., Wang, L., & Li, Y. (2025) · Chemical Biology & Drug Design · doi:10.1111/cbdd.70148 · Cited by 4

The combined association of the neutrophil percentage-to-albumin ratio (NPAR) and the uric acid-to-high-density lipoprotein cholesterol ratio (UHR) with adverse cardiac events in patients with chronic heart failure: a retrospective cohort study

Fu, Y. S., Song, G., Wu, S., Ma, L., Bao, X., Liu, X., & Gu, R. (2025) · Lipids in Health and Disease · doi:10.1186/s12944-025-02807-z · Cited by 4

Computer-Aided Drug Design of Plant-Based Compounds

Bıçak, B., & Kecel‐Gunduz, S. (2022) · Advances in bioinformatics and biomedical engineering book series · doi:10.4018/978-1-6684-7337-5.ch013 · Cited by 4

Efficacy and in vitro pharmacological assessment of novel N -hydroxypyridinediones as hepatitis B virus ribonuclease H inhibitors

Woodson, M. E., Walden, H. F., Mottaleb, M. A., Makri, M., Prifti, G., Moianos, D., Pardali, V., Zoidis, G., & Tavis, J. E. (2024) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01455-24 · Cited by 4

DHEA-carbamate derivatives as dual cholinesterase inhibitors: Integration of enzymatic and biomolecular interactions in Alzheimer's disease

Nar, K., Erdağı, S. İ., & Ozbagci, D. I. (2025) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2025.108901 · Cited by 4

Plasma protein binding of cannabidiol

Lara, J., Schweky, N., & Babayeva, M. (2022) · Phytotherapy Research · doi:10.1002/ptr.7443 · Cited by 4

Statistical Methods in the Study of Protein Binding and Its Relationship to Drug Bioavailability in Breast Milk

Wanat, K., & Brzezińska, E. (2022) · Molecules · doi:10.3390/molecules27113441 · Cited by 4

Electrochemical and CD-spectroelectrochemical studies of the interaction between BSA and the complex [Cu(Bztpen)]2+, (Bztpen = (N-benzyl-N, N′, N′-tris (pyridin-2-ylmethyl) ethylenediamine)

Ocampo-Hernández, J., Gómez-Guzmán, J. D. J., Cruz-Ramírez, M., Rebolledo‐Chávez, J. P. F., Mendoza, Á., Moreno‐Esparza, R., & Ortiz-Frade, L. (2022) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2022.111994 · Cited by 4

Molecular docking of human serum albumin with penicillin G determinants

Khmil, N. V., & Kolesnikov, V. G. (2023) · Biophysical Bulletin · doi:10.26565/2075-3810-2023-49-01 · Cited by 4

Determination of 3- and 4-chloromethcathinone interactions with plasma proteins: study involving analytical and theoretical methods

Hołowiński, P., & Dybowski, M. P. (2023) · Forensic Toxicology · doi:10.1007/s11419-023-00677-7 · Cited by 4

A Pharmacological Investigation of the TMEM16A Currents in Murine Skeletal Myogenic Precursor Cells

Sciancalepore, M., Ragnini, A., Zacchi, P., Borelli, V., D’Andrea, P., Lorenzon, P., & Bernareggi, A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25042225 · Cited by 4

Human Serum Albumin Structure in Presence of Different Concentrations of Cortisol and Glucose: An In Vitro Modeling Under Normal and Hyperglycemic Conditions

Amini-Geram, P., Goshadrou, F., Ebrahim‐Habibi, A., Yaghmaei, P., & Tackallou, S. H. (2016) · Iranian Red Crescent Medical Journal · doi:10.5812/ircmj.40306 · Cited by 4

Complexation of cis-Pt and trans-Pt(NH3)2Cl2 with serum proteins: A potential application for drug delivery

Chanphai, P., Bariyanga, J., Bérubé, G., & Tajmir‐Riahi, H. A. (2019) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2019.1654408 · Cited by 4

Modification of blood serum DSC profiles by sauna treatments in cross-country skiers during the exercise cycle

Duch, K., Michnik, A., Pokora, I., & Sadowska‐Krępa, E. (2020) · Journal of Thermal Analysis and Calorimetry · doi:10.1007/s10973-020-10162-7 · Cited by 4

Lauroyl hyaluronan films for local drug delivery: Preparation and factors influencing the release of small molecules

Chmelař, J., Brtková, B., Laštovičková, L., Bažantová, J., Hermannová, M., Kulhánek, J., Mrázek, J., & Velebný, V. (2021) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2021.121111 · Cited by 4

Considerations for drug–drug interactions between long-acting antiretrovirals and immunosuppressants for solid organ transplantation

Coppinger, C., & Anderson, P. L. (2024) · Expert Opinion on Drug Metabolism & Toxicology · doi:10.1080/17425255.2024.2448970 · Cited by 4

Human Serum Albumin Grafted by Monomeric and Polymeric β-Cyclodextrin as Drug Delivery System for Levofloxacin with Improved Pharmacological Properties

Kopnova, T. Y., Yakupova, L. R., Belogurova, N. G., & Kudryashova, E. V. (2024) · Future Pharmacology · doi:10.3390/futurepharmacol4010010 · Cited by 3

Spectroscopic study on volasertib: Highly stable complexes with albumin and encapsulation into alginate/montmorillonite bionanocomposites

Fernández-Sainz, J., Herrera‐Ochoa, D., Pacheco-Liñán, P. J., Darder, M., Albaladejo, J., Bravo, I., & Garzón‐Ruiz, A. (2024) · Spectrochimica Acta Part A Molecular and Biomolecular Spectroscopy · doi:10.1016/j.saa.2024.124823 · Cited by 3

Distinctive hydrogen binding interactions enable fluorescent sensor to Discriminate HSA from BSA in fluorescent sensing

Qiao, Y., Cao, J., Li, Y., Wang, C., Gao, J., Wang, L., Sun, W., Wang, L., Li, Y., & Zuo, Z. (2025) · Microchemical Journal · doi:10.1016/j.microc.2025.114159 · Cited by 3

Molecular Interactions of Cobimetinib and Vemurafenib with Human Serum Albumin: a Comparative Biophysical and Computational Analysis

Cavalieri, G., Marson, D., Starz, A., Laurini, E., & Pricl, S. (2025) · Molecular Pharmaceutics · doi:10.1021/acs.molpharmaceut.5c00625 · Cited by 3

Single-chain variable fragments targeting domain II of human serum albumin for enhanced circulatory half-life via albumin association

Park, A.-R., Jung, E.-Y., Shin, H. H., Park, J., Lim, S. I., & Lee, D. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.146933 · Cited by 3

Site-Specific Binding of Anti-Cancer Drugs to Human Serum Albumin

Bhosale, M., Jeelani, I., Nawaz, A., Abe, H., & Padhyé, S. (2022) · Anti-Cancer Agents in Medicinal Chemistry · doi:10.2174/1871520622666220324094033 · Cited by 3

Cyclodextrin-Based Displacement Strategy of Sterigmatocystin from Serum Albumin as a Novel Approach for Acute Poisoning Detoxification

Jakšić, D., Klarić, M. Š., Rimac, H., Kerep, R., & Piantanida, I. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24054485 · Cited by 3

In Vitro Study of the Interaction between Ochratoxin A and Human Serum Albumin by Spectroscopic and Molecular Docking Methods

Vakili, S., Baher, E., Vaezi, Z., Mianabadi, M., & Tilami, S. E. (2023) · ChemistrySelect · doi:10.1002/slct.202301310 · Cited by 3

Effects of ultraviolet radiation and reactive oxygen species on the structure and ligand-binding ability of human serum albumin for norfloxacin

Zhang, J., Ma, Q., Li, Y., Liao, Y., & Wang, H. (2024) · Journal of Molecular Liquids · doi:10.1016/j.molliq.2024.124688 · Cited by 3

Interaction Studies of Metal-Based Anticancer Drug Entities with Potential Therapeutic Targets

Arjmand, F., Tabassum, S., & Khan, H. Y. (2024) · Springer eBooks · doi:10.1007/978-981-97-0146-9_3 · Cited by 3

Experimental and computational perspectives on the interaction of nerve agent VX metabolite ethyl methylphosphonic acid with human serum albumin

Bakırhan, N. K., Brahmi, M., Gündüz, M. G., Kaya, S. I., Sezigen, S., & Özkan, S. A. (2024) · Microchemical Journal · doi:10.1016/j.microc.2024.111406 · Cited by 3

Tailoring Soft Nanoparticles for Potential Application as Drug Carriers in Bladder Cancer Chemotherapy

Neoh, K. G., Lu, S., Kang, E. T., Mahendran, R., & Chiong, E. (2016) · ACS symposium series · doi:10.1021/bk-2016-1224.ch009 · Cited by 3

Collective Excitations in Protein as a Measure of Balance Between its Softness and Rigidity

Shrestha, U. R., Bhowmik, D., Delinder, K. W. V., Mamontov, E., O’Neill, H., Zhang, Q., Alatas, A., & Chu, X.-Q. (2017) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.6b10245 · Cited by 3

Ajwain-assisted synthesis of oxalipalladium nanoparticles for colorectal cancer treatment: enhanced anticancer activity and protein interaction profiling

Goli, F., Divsalar, A., Rasouli, M., & Gholami, H. R. (2024) · New Journal of Chemistry · doi:10.1039/d4nj02391a · Cited by 2

Interactive Associations of Drug–Drug and Drug–Drug–Drug with IIA Subdomain of Human Serum Albumin

Yang, F., Yue, J., Ma, L., Ma, Z., Li, M., Wu, X., & Liang, H. (2012) · Molecular Pharmaceutics · doi:10.1021/mp300322y · Cited by 56

Studies on Drug – Human Serum Albumin Binding: The Current State of the Matter

Zhivkova, Z. D. (2015) · Current Pharmaceutical Design · doi:10.2174/1381612821666150302113710 · Cited by 112

Structural Basis of Drug Recognition by Human Serum Albumin

Leboffe, L., di Masi, A., Polticelli, F., Trezza, V., & Ascenzi, P. (2019) · Current Medicinal Chemistry · doi:10.2174/0929867326666190320105316 · Cited by 66

Unraveling the versatility of human serum albumin – A comprehensive review of its biological significance and therapeutic potential

Ashraf, S., Qaiser, H., Tariq, S., Khalid, A., Makeen, H. A., Alhazmi, H. A., & Ul‐Haq, Z. (2023) · Current Research in Structural Biology · doi:10.1016/j.crstbi.2023.100114 · Cited by 118

A mini review on human serum albumin - natural alkaloids interaction and its role as drug carrier

Ghosh, T., & Bhadra, K. (2024) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2024.2314254 · Cited by 28