Article
Chemistry, Physical
Levente Tyukodi, Balazs Zoltan Zsido, Csaba Hetenyi, Tamas Koszegi, Imre Huber, Zsuzsanna Rozmer
Summary: In this study, the binding nature of three selected synthetic cyclic C5-curcuminoid derivatives to human serum albumin (HSA) at different temperatures was investigated using UV-Vis absorption spectroscopy, fluorescence methods, and 3D molecular modeling simulation. The experimental results revealed that the compounds formed complexes with HSA, leading to fluorescence quenching through a predominantly static quenching process with a quenching constant in the range of 104-105 M-1. The binding constants, binding sites, and thermodynamic parameters were calculated, suggesting that hydrophobic forces played a major role in the interaction between curcuminoids and HSA.
JOURNAL OF MOLECULAR STRUCTURE
(2023)
Article
Biochemical Research Methods
Parsa Bazdar, Ali R. Jalalvand, Vali Akbari, Reza Khodarahmi, Hector C. Goicoechea
Summary: This article discusses the investigation of interactions between miglitol and normal human serum albumin and glycated HSA, using spectroscopic and electrochemical data. Chemometric methods were employed to extract useful information for justifying these interactions, and molecular docking techniques were used for further investigation. A novel chemometrics-assisted electroanalytical method was developed for diagnostic and monitoring of diabetes.
ANALYTICAL BIOCHEMISTRY
(2021)
Review
Chemistry, Analytical
Jian-Fei Xu, Yu-Shun Yang, Ai-Qin Jiang, Hai-Liang Zhu
Summary: This review highlights the importance of human serum albumin (HSA) and its association with various diseases. It provides an overview of HSA detection methods, including traditional dye-binding and immune methods, as well as emerging technologies such as fluorescent probe detection and biosensors. Additionally, the review emphasizes the research progress of small molecular fluorescence probe method. The challenges and future directions in the field of HSA detection are also briefly discussed.
CRITICAL REVIEWS IN ANALYTICAL CHEMISTRY
(2022)
Article
Biochemistry & Molecular Biology
Umesha Katrahalli, Govindaswamy Shanker, Debnath Pal, Manjunatha Devagondanahalli Hadagali
Summary: This study investigated the binding characteristics of the water-soluble thiadicarbocyanine dye DTC with BSA using spectroscopic techniques and molecular docking methods. The experimental results showed that DTC quenched the fluorescence intensity of BSA and altered its secondary structure. The binding was found to be driven by hydrophobic forces. Molecular docking validated the experimental findings and revealed a free binding energy release of -7.37 kcal/mol. This research provides insights into the interaction between water-soluble DTC dye and biological molecules.
JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS
(2022)
Article
Optics
Sony Udayan, Drishya Elizebath, D. R. Sherin, Vakayil K. Praveen, Sini Sunny, Purushothaman Jayamurthy, T. K. Manojkumar, V. P. N. Nampoori, Sheenu Thomas
Summary: This study demonstrates the use of a hexamethine hemicyanine dye as a thermo-optical probe for serum albumin, revealing significant alterations in optical and thermal properties upon binding with the protein. Spectroscopic techniques and molecular docking methods were utilized to investigate the interaction between the dye and serum albumin, indicating enhanced stability of proteins and reduced thermal diffusivity of the dye when bound with the albumin.
OPTICS AND LASER TECHNOLOGY
(2021)
Article
Spectroscopy
Jie Bai, Xuekai Sun, Bing Geng, Xiping Ma
Summary: FTIR, fluorescence, and UV-vis absorption techniques were used to study the interaction between Cu+ and Cu2+ and bovine serum albumin (BSA) under simulated physiological conditions. The spectroscopic analysis showed that Cu+/Cu2+ could quench the intrinsic fluorescence emitted by BSA through static quenching with binding sites of 0.88 and 1.12 for Cu+ and Cu2+ respectively. The interaction was mainly driven by electrostatic force, as indicated by the negative ΔH and positive ΔS values. This study provides insight into the toxicological effects of different speciation of copper at the molecular level.
SPECTROCHIMICA ACTA PART A-MOLECULAR AND BIOMOLECULAR SPECTROSCOPY
(2023)
Review
Biochemistry & Molecular Biology
Vibhor Mishra, Richard J. Heath
Summary: Serum albumin interacts with various substances, functions as a critical transporter, and scavenges reactive oxygen species, making it a suitable choice to promote cell growth and survival in vitro culture.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2021)
Review
Pharmacology & Pharmacy
Aziz Ullah, Goeun Shin, Sung In Lim
Summary: This review evaluates the current state of knowledge regarding various aspects of ABMs and the unique advantages of ABM-mediated drug delivery. It also discusses how ABMs can be specifically modulated to maximize potential benefits in clinical development.
DRUG DISCOVERY TODAY
(2023)
Article
Biochemistry & Molecular Biology
Jijing Wang, Susanna L. Lundstrom, Sven Seelow, Sergey Rodin, Zhaowei Meng, Juan Astorga-Wells, Qinyu Jia, Roman A. Zubarev
Summary: A novel monoclonal antibody 1A3 with excellent specificity to isoAsp in the functionally important domain of HSA was developed, leading to the quantification of isoAsp occupancy in 100 healthy plasma samples. These results suggest the potential of isoAsp measurements for supplementary AD diagnostics and assessing the freshness of stored donor blood for transfusion suitability.
Article
Chemistry, Multidisciplinary
Sarah McColman, Rui Li, Selena Osman, Amanda Bishop, Kathleen P. Wilkie, David T. Cramb
Summary: This study used Fluorescence Correlation/Cross Correlation Spectroscopy and Fluorescence Resonance Energy Transfer to directly analyze four different nanoparticle systems, finding surface heterogeneity to be a key factor in protein binding to these nanoparticles. The early hard corona is conceptualized as low-ratio, non-uniform binding rather than a uniform monolayer.
Article
Chemistry, Multidisciplinary
Sangeetha Murugan Sreedevi, Seba Merin Vinod, Anju Krishnan, Tamizhdurai Perumal, Fatmah Ali Alasmary, Norah Salem Alsaiari, Mani Govindasamy, Kumaran Rajendran
Summary: Molecular docking studies were conducted to investigate the binding stability and feasibility of resorcinol-based acridinedione dyes (ADR1 and ADR2) with a globular protein, Human Serum Albumin (HSA). The results showed that ADR2 dye had a more stable and feasible binding with HSA compared to ADR1 dye. ADR1 dye predominantly bound to site I and III of HSA and acted as a hydrogen bonding acceptor, while ADR2 dye bound to all binding sites and acted as a hydrogen bonding donor. The importance of drug-governance on the binding affinity of dye-protein complex was also studied. Site I binding drugs decreased the binding affinity of ADR1 dye-HSA complex, while site II binding drugs predominantly decreased the affinity of ADR2 dye-HSA complex. The study highlights the utility of molecular docking in understanding the stability and binding of host-guest complexes. Rating: 8 out of 10.
ARABIAN JOURNAL OF CHEMISTRY
(2023)
Editorial Material
Oncology
Guus A. M. S. van Dongen
Summary: The high affinity of an antibody can lead to restricted tumor penetration and heterogeneous distribution, limiting the efficacy of antibody-based therapies. By competitively inhibiting antibody-antigen binding, increased tumor penetration of the antibody and enhanced efficacy of ADCs can be achieved.
Article
Biochemistry & Molecular Biology
Sharat Sarmah, Somdev Pahari, Sourav Das, Vinay Kumar Belwal, Madhurima Jana, Atanu Singha Roy
Summary: The non-enzymatic glycation of plasma proteins significantly reduces the binding affinity of HSA towards chrysin, while the % alpha-helicity of HSA is enhanced upon binding with chrysin. Chrysin mainly binds to subdomain IIA and IIIA of both HSA and gHSA in the interaction study.
JOURNAL OF BIOMOLECULAR STRUCTURE & DYNAMICS
(2021)
Article
Biochemistry & Molecular Biology
Satsuki Obara, Keita Nakane, Chizu Fujimura, Shusuke Tomoshige, Minoru Ishikawa, Shinichi Sato
Summary: This study developed a tyrosine-selective modification method for HSA, with laccase-catalyzed method being able to efficiently introduce functional groups under mild conditions. Mass spectrometry analysis identified Y84, Y138, and Y401 as the main modification sites.
INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
(2021)
Article
Chemistry, Medicinal
Thomas B. Kjeldsen, Frantisek Hubalek, Claudia U. Hjorringgaard, Tina M. Tagmose, Erica Nishimura, Carsten E. Stidsen, Trine Porsgaard, Christian Fledelius, Hanne H. F. Refsgaard, Sanne Gram-Nielsen, Helle Naver, Lone Pridal, Thomas Hoeg-Jensen, Claus Bekker Jeppesen, Valentina Manfe, Svend Ludvigsen, Inger Lautrup-Larsen, Peter Madsen
Summary: The molecular engineering of insulin icodec has resulted in a plasma half-life of 196 hours in humans, suitable for once-weekly subcutaneous administration. In a phase-2 clinical trial, it demonstrated safe and efficacious glycemic control comparable to once-daily insulin glargine in type 2 diabetes patients, showing the potential of insulin icodec as a long-acting therapeutic option.
JOURNAL OF MEDICINAL CHEMISTRY
(2021)