Journal of Molecular Recognition最新文献

{"title":"Integrated spectroscopic and computational analyses unravel the molecular interaction of pesticide azinphos-methyl with bovine beta-lactoglobulin","authors":"Nasser Abdulatif Al-Shabib,&nbsp;Javed Masood Khan,&nbsp;Ajamaluddin Malik,&nbsp;Abdulaziz AlAmri,&nbsp;Md Tabish Rehman,&nbsp;Mohamed F. AlAjmi,&nbsp;Fohad Mabood Husain","doi":"10.1002/jmr.3086","DOIUrl":"10.1002/jmr.3086","url":null,"abstract":"<p>Organophosphorus are typically hazardous chemicals used in the pharmaceutical, agricultural, and other industries. They pose a serious risk to human life and can be fatal upon direct exposure. Hence, studying the interaction between such compounds with proteins is crucial for environmental, health, and food safety. In this study, we investigated the interaction mechanism between azinphos-methyl (AZM) and β-lactoglobulin (BLG) at pH 7.4 using a combination of biophysical techniques. Intrinsic fluorescence investigations revealed that BLG fluorescence was quenched in the presence of increasing AZM concentrations. The quenching mechanism was identified as static, as evidenced by a decrease in the fluorescence quenching constant (1.25 × 10⁴, 1.18 × 10⁴, and 0.86 × 10⁴ M⁻¹) with an increase in temperatures. Thermodynamic calculations (Δ<i>H</i> &gt; 0; Δ<i>S</i> &gt; 0) affirmed the formation of a complex between AZM and BLG through hydrophobic interactions. The BLG's secondary structure was found to be increased due to AZM interaction. Ultraviolet –visible spectroscopy data showed alterations in BLG conformation in the presence of AZM. Molecular docking highlighted the significant role of hydrophobic interactions involving residues such as Val43, Ile56, Ile71, Val92, Phe105, and Met107 in the binding between BLG and AZM. A docking energy of −6.9 kcal mol⁻¹, and binding affinity of 1.15 × 10⁵ M⁻¹ suggest spontaneous interaction between AZM and BLG with moderate to high affinity. These findings underscore the potential health risks associated with the entry of AZM into the food chain, emphasizing the need for further consideration of its impact on human health.</p>","PeriodicalId":16531,"journal":{"name":"Journal of Molecular Recognition","volume":"37 4","pages":""},"PeriodicalIF":2.7,"publicationDate":"2024-04-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140830372","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Dual template (epitope) imprinted electrode for sensing bacterial protein with high selectivity","authors":"Akriti Srivastava,&nbsp;Manjeet Harijan,&nbsp;Rajniti Prasad,&nbsp;Meenakshi Singh","doi":"10.1002/jmr.3087","DOIUrl":"10.1002/jmr.3087","url":null,"abstract":"<p>Epitope imprinting has shown better prospects to synthesize synthetic receptors for proteins. Here, dual epitope imprinted polymer electrode (DEIP) matrix was fabricated on gold surface of electrochemical quartz crystal microbalance (EQCM) for recognition of target epitope sequence in blood samples of patients suffering from brain fever. Epitope sequences from outer membrane protein Por B of <i>Neisseria meningitidis</i> (MC58) bacteria predicted through immunoinformatic tools were chosen for imprinting. Self-assembled monolayers (SAM) of cysteine appended epitope sequences on gold nanoparticles were subjected to polymerization prior to electrodeposition on gold coated EQCM electrode. The polymeric matrix was woven around the cysteine appended epitope SAMs through multiple monomers (3-sulfo propyl methacrylate potassium salt (3-SPMAP), benzyl methacrylate (BMA)) and crosslinker (N, N′-methylene-<i>bis</i>-acrylamide). On extraction of the peptide sequences, imprinted cavities were able to selectively and specifically bind targeted epitope sequences in laboratory samples as well as ‘real’ samples of patients. Selectivity of sensor was examined through mismatched peptide sequences and certain plasma proteins also. The sensor was able to show specific binding towards the blood samples of infected patients, even in the presence of ‘matrix’ and other plasma proteins such as albumin and globulin. Even other peptide sequences, similar to epitope sequences only with one or two amino acid mismatches were also unable to show any binding. The analytical performance of DEIP-EQCM sensor was tested through selectivity, specificity, matrix effect, detection limit (0.68–1.01 nM), quantification limit (2.05–3.05 nM) and reproducibility (RSD ~ 5%). Hence, a diagnostic tool for bacterium causing meningitis is successfully fabricated in a facile manner which will broaden the clinical access and make efficient population screening feasible.</p>","PeriodicalId":16531,"journal":{"name":"Journal of Molecular Recognition","volume":"37 4","pages":""},"PeriodicalIF":2.7,"publicationDate":"2024-04-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140830361","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Dissimilar effects of the hydrophilic carbon dots on the amyloid aggregation of two model proteins and the mechanism discussion","authors":"Jie Li,&nbsp;Yuangong Zhang,&nbsp;Jiawei Dong,&nbsp;Dexin Li,&nbsp;Xinwu Ba,&nbsp;Sujuan Wang","doi":"10.1002/jmr.3085","DOIUrl":"10.1002/jmr.3085","url":null,"abstract":"<p>Many proteins could aggregate into amyloid fibrils under certain conditions. However, the aggregation process and morphology of the fibrils may be significantly different because of the distinct protein structure. In this article, the hydrophilic carbon dots (Lys-CA-CDs) were prepared using lysine (Lys) and citric acid (CA) as reactant under the assistance of a microwave. The dissimilar modulation effect of Lys-CA-CDs on the aggregation process of distinct structure protein was further investigated, where bovine serum albumin (BSA) and hen egg white lysozyme (HEWL) were chosen as model proteins. All results showed that Lys-CA-CDs displayed the contrary influence on the aggregation process of BSA and HEWL. Lys-CA-CDs could induce BSA to aggregate into more wormlike fibrils and inhibit the aggregation of HEWL into hair-like fibrils. The influence on the aggregation process of BSA may be assigned to the increased concentration of BSA around the Lys-CA-CDs caused by their interaction. However, inserting of Lys-CA-CDs into the inner structure of HEWL led to the change of protein secondary structure. The change of secondary structure further made it difficult for HEWL to aggregate into fibrils and Lys-CA-CDs showed the inhibition effect on HEWL aggregation.</p>","PeriodicalId":16531,"journal":{"name":"Journal of Molecular Recognition","volume":"37 4","pages":""},"PeriodicalIF":2.7,"publicationDate":"2024-04-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140592227","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Exploring the interaction of a potent anti-cancer drug Selumetinib with bovine serum albumin: Spectral and computational attributes","authors":"Ankita Jalan,&nbsp;Satyam Sangeet,&nbsp;Amit Kumar Pradhan,&nbsp;N. Shaemningwar Moyon","doi":"10.1002/jmr.3084","DOIUrl":"10.1002/jmr.3084","url":null,"abstract":"<p>The binding of drugs to plasma proteins determines its fate within the physiological system, hence profound understanding of its interaction within the bloodstream is important to understand its pharmacodynamics and pharmacokinetics and thereby its therapeutic potential. In this regard, our work delineates the mechanism of interaction of Selumetinib (SEL), a potent anti-cancer drug showing excellent effect against multiple solid tumors, with plasma protein bovine serum albumin (BSA), using methods such as absorption, steady-state fluorescence, time-resolved, fluorescence resonance energy transfer, Fourier transform infrared spectra (FTIR), circular dichroism (CD), synchronous and 3D-fluorescence, salt fluorescence, molecular docking and molecular dynamic simulations. The BSA fluorescence intensity was quenched with increasing concentration of SEL which indicates interactions of SEL with BSA. Stern–Volmer quenching analysis and lifetime studies indicate the involvement of dynamic quenching. However, some contributions from the static quenching mechanism could not be ruled out unambiguously. The association constant was found to be 5.34 × 10⁵ M⁻¹ and it has a single binding site. The Förster distance (r) indicated probable energy transmission between the BSA and SEL. The positive entropy changes and enthalpy change indicate that the main interacting forces are hydrophobic forces, also evidenced by the results of molecular modeling studies. Conformation change in protein framework was revealed from FTIR, synchronous and 3D fluorescence and CD studies. Competitive binding experiments as well as docking studies suggest that SEL attaches itself to site I (subdomain IIA) of BSA where warfarin binds. Molecular dynamic simulations indicate the stability of the SEL–BSA complex. The association energy between BSA and SEL is affected in the presence of different metals differently.</p>","PeriodicalId":16531,"journal":{"name":"Journal of Molecular Recognition","volume":"37 4","pages":""},"PeriodicalIF":2.7,"publicationDate":"2024-04-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140591983","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Some pyrroles as inhibitors of the pentose phosphate pathways enzymes: An in vitro and molecular docking study","authors":"Muhammet Serhat Özaslan","doi":"10.1002/jmr.3083","DOIUrl":"10.1002/jmr.3083","url":null,"abstract":"<p>Glucose-6-phosphate dehydrogenase (G6PD) and 6-phosphogluconate dehydrogenase (6PGD) are pentose phosphate pathway enzymes. Compounds with a heterocyclic pyrrole ring system containing this atom can be derivatized with various functional groups into highly effective bioactive agents. In this study, pyrrole derivatives on these enzyme's activity were investigated. The IC₅₀ values of different concentrations of pyrrole derivatives for G6PD were found in the range of 0.022–0.221 mM <i>K</i>_i values 0.021 ± 0.003–0.177 ± 0.021 and for 6PGD IC₅₀ values 0.020–0.147, mM <i>K</i>_i values 0.013 ± 0.002–0.113 ± 0.030 mM. The 2-acetyl-1-methylpyrrole (<b>1g</b>) showed the best inhibition value for G6PD and 6PGD enzymes. In addition, in silico molecular docking experiments were performed to elucidate how these pyrrole derivatives (<b>1a</b>–<b>g</b>) interact with the binding sites of the target enzymes. The study's findings on pyrrole derivatives could be used to create innovative therapeutics that could be a treatment for many diseases, especially cancer manifestations.</p>","PeriodicalId":16531,"journal":{"name":"Journal of Molecular Recognition","volume":"37 3","pages":""},"PeriodicalIF":2.7,"publicationDate":"2024-03-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140184709","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Insights into the G-quadruplex DNA interaction landscape: Comparative analysis of anionic Zn(II) and Co(II) phthalocyanine-tetrasulfonate complexes","authors":"Efkan Bağda","doi":"10.1002/jmr.3082","DOIUrl":"10.1002/jmr.3082","url":null,"abstract":"<p>G-quadruplexes play a pivotal role in regulating various cellular processes, including gene expression and replication, making them essential structures in understanding, and manipulating cellular functions. The development of G-quadruplex ligands holds significant promise in therapeutic and research applications, offering targeted tools to modulate G-quadruplex structures and potentially influence critical biological pathways. An exciting frontier in G-quadruplex research lies in the exploration of anionic ligands, and their profound impact on stabilizing and modulating G-quadruplex DNA. In this study, the interaction of two anionic phthalocyanine compounds (Zinc (II) phthalocyanine 3,4′,4″,4‴-tetrasulfonic acid, tetrasodium salt, <b>ZnAPC</b>; cobalt (II) phthalocyanine 3,4′,4″,4‴-tetrasulfonic acid, tetrasodium salt, <b>CoAPC</b>) and three separate G-quadruplex-forming DNA sequences was investigated. Interactions were carried out by DNA polymerase stop studies along with spectroscopic studies. According to the results of experimental data, it was determined that <b>ZnAPC</b> actively interacts with the G-quadruplex DNA structures. On the other hand, it was thought that the interaction with <b>CoAPC</b> was less and even occurred in simple electrostatic interactions. K_D constants and B_max constants for the interaction with <b>ZnAPC</b> were calculated. The K_D constants for <b>ZnAPC</b> were found to be (1.16 ± 0.07) × 10⁻⁵, (9.75 ± .24) × 10⁻⁶ and (1.00 ± 0.36) × 10⁻⁴ M for AS1411, Vegf, and Tel21, respectively. Accordingly, it was concluded that <b>ZnAPC</b> interacts with G-quadruplex DNA ligands effectively.</p>","PeriodicalId":16531,"journal":{"name":"Journal of Molecular Recognition","volume":"37 3","pages":""},"PeriodicalIF":2.7,"publicationDate":"2024-03-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140110516","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Editorial: The Journal of Molecular Recognition: Changing of the guard","authors":"Rebecca C. Wade","doi":"10.1002/jmr.3081","DOIUrl":"10.1002/jmr.3081","url":null,"abstract":"&lt;p&gt;At the beginning of 2024, I took over from Marc van Regenmortel as the third Editor-in-Chief of JMR. The journal was established by Irwin Chaiken in 1988 with affiliation to the International Society for Molecular Recognition (ismr.org) and with a strong focus on methods to measure affinity. Presciently, and quite unusually, the journal was founded to focus on a phenomenon—molecular recognition—and it is a phenomenon that is central to biomolecular science. This has enabled the content of the journal to evolve over time as new techniques, ideas, and applications have emerged. In 1999, Marc van Regenmortel became Editor-in-Chief, introduced new types of articles, and broadened the scope of the journal. For example, the series of comprehensive critical reviews on methods, such as surface plasmon resonance, isothermal calorimetry, and molecular docking, were particularly well read. We, the editors and advisory board members, thank him for his vision, inspiration, dedication, and hard work in successfully steering the journal over the last 25 years. He leaves the journal on solid foundations, publishing on a broad range of molecular recognition topics. Marc sought to make the journal, not only THE place to publish high-quality research on molecular recognition but also a venue for discussion on concepts and controversial issues relating to molecular recognition. We will continue to pursue these aims. For this purpose, we are introducing an additional article category called “Perspective” for short articles with commentaries, discussions, or reviews on current topics. The first two Perspectives are on Marc's contributions to science and the scientific community&lt;span&gt;&lt;sup&gt;1, 2&lt;/sup&gt;&lt;/span&gt; and highly recommended reading. We will also aim to nurture the broad community of molecular recognition researchers, for example, through awards at conferences and with the establishment of a new Early Career Advisory Board for the journal.&lt;/p&gt;&lt;p&gt;Now is an appropriate time for JMR to enter into its third epoch. The growing prominence of computational science and the dramatic advances in artificial intelligence are changing how research into molecular recognition is done. This is reflected in the appointment of a theoretical and computational scientist at the helm of JMR. Moreover, the panel of Associate Editors includes two theoreticians as well as other scientists who combine computation with their experimental work. We will be looking to see how artificial intelligence and data science complement our existent methodological toolbox to accelerate molecular recognition research and enable the discovery of new molecules, new binding mechanisms, and new conceptual insights. However, in all the excitement over the new possibilities that such approaches bring, it is important to ensure that computational and machine learning tools and techniques are applied rigorously and carefully, with experimental validation whenever possible. Moreover, we expect that AI will be a","PeriodicalId":16531,"journal":{"name":"Journal of Molecular Recognition","volume":"37 3","pages":""},"PeriodicalIF":2.7,"publicationDate":"2024-03-11","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/jmr.3081","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140101756","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Marc van Regenmortel, personal recollections on a forward-thinking editor","authors":"Jean-Luc Pellequer,&nbsp;Eric Westhof","doi":"10.1002/jmr.3080","DOIUrl":"10.1002/jmr.3080","url":null,"abstract":"<p>Marc van Regenmortel was the Editor-in-Chief of the Journal of Molecular Recognition for the last 25 years. Without attempting to summarize Marc's exceptional career and achievements, we would like to tell the story of the tortuous and contingent path to the unravelling of a key molecular recognition process in antigenicity. Life is indeed full of contingencies and scientific life, full of meetings and random encounters, is prone to contingencies, a key element in discovery and innovation.</p>","PeriodicalId":16531,"journal":{"name":"Journal of Molecular Recognition","volume":"37 3","pages":""},"PeriodicalIF":2.7,"publicationDate":"2024-03-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/jmr.3080","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140028253","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Marc H. V. van Regenmortel, a virtual friend and a real colleague","authors":"Vladimir N. Uversky","doi":"10.1002/jmr.3079","DOIUrl":"10.1002/jmr.3079","url":null,"abstract":"&lt;p&gt;Unlike Jean-Luc Pellequer and Eric Westhof,&lt;span&gt;&lt;sup&gt;1&lt;/sup&gt;&lt;/span&gt; who were colleagues of Marc H.V. van Regenmortel, I have never met him in person. However, I can add my voice to the discussion of how contingency or serendipity has led me to productively collaborate with Marc (unfortunately, exclusively in the on-line format), resulting in the publication of a joint paper in 2020.&lt;span&gt;&lt;sup&gt;2&lt;/sup&gt;&lt;/span&gt; Before moving to this part of my story, a short historical excurse is needed.&lt;/p&gt;&lt;p&gt;My first (once again, exclusively virtual) encounter with Marc took place in 2004, when he played a crucial role in our work on one of the first comprehensive reviews on the roles of intrinsically disordered proteins and regions (IDPs/IDRs) in molecular recognition, regulation, and cell signaling.&lt;span&gt;&lt;sup&gt;3&lt;/sup&gt;&lt;/span&gt; In the middle of 2004, I joined the Center for Computational Biology and Bioinformatics (CCBB) at the Indiana University-Purdue University at Indianapolis (IUPUI) that was created and headed by Prof. A. Keith Dunker, whom I worked with for 6 years on different aspects of the protein intrinsic disorder phenomenon. One of my first projects there was analysis of the then-available literature data on the functionality of intrinsic disorder.&lt;/p&gt;&lt;p&gt;By that time, it became clear that although IDPs/IDRs have been mostly ignored by the scientific community since the inception of the lock-and-key model by Hermann Emil Louis Fischer (1852–1919) in 1894,&lt;span&gt;&lt;sup&gt;4, 5&lt;/sup&gt;&lt;/span&gt; many aspects of protein functionality could not be explained using this important model and its associated sequence-structure-function paradigm. In fact, many protein functions do not require specific structures, instead relying on conformational flexibility, and as a result, many biologically active proteins (or protein regions) do not have unique structures, instead being intrinsically disordered.&lt;span&gt;&lt;sup&gt;6-15&lt;/sup&gt;&lt;/span&gt; However, the concept of functional disorder was still met with strong skepticism by the scientific community, especially by those who worked in structural biology.&lt;/p&gt;&lt;p&gt;This brings us to my first example of Marc-centric contingency or serendipity. When Keith contacted Marc to check if the manuscript we were working on would fit the scope of the Journal of Molecular Recognition, to our big surprise, we received very enthusiastic support. Those times were still the early days of protein intrinsic disorder, and many scientific journals were simply dismissing the idea of functional disorder as nonsensical (as an example, it took more than a year to publish my first paper on this subject (Ref. &lt;span&gt;16&lt;/span&gt;), which was rejected by 14 journals before being eventually accepted by Proteins&lt;span&gt;&lt;sup&gt;7&lt;/sup&gt;&lt;/span&gt;). During the preparation of the manuscript for the Journal of Molecular Recognition, we had a productive exchange with Marc, which was very useful and is reflected in the acknowledgement in the resulting paper that reads “Both A.K.D. and V.N.U. t","PeriodicalId":16531,"journal":{"name":"Journal of Molecular Recognition","volume":"37 3","pages":""},"PeriodicalIF":2.7,"publicationDate":"2024-02-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/jmr.3079","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139990347","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Tenth International AFMBioMed Conference on AFM in Life Sciences and Medicine, August 30–September 2, 2022, Nagoya-Okasaki, Japan","authors":"Takayuki Uchihashi,&nbsp;Felix Rico,&nbsp;Jean-Luc Pellequer","doi":"10.1002/jmr.3077","DOIUrl":"10.1002/jmr.3077","url":null,"abstract":"&lt;p&gt;Founded in June 2006, after a first seminal French-speaking conference held on the topic “Atelier Nanobiosciences: protéines et membranes” in &lt;i&gt;Nîmes&lt;/i&gt; in June 2004, the AFMBioMed Conference brings researchers and students from around the world together to discuss the latest scientific results of atomic force microscopy in life sciences and medicine.&lt;span&gt;&lt;sup&gt;1, 2&lt;/sup&gt;&lt;/span&gt; A full account of the AFMBioMed history can be found here.&lt;span&gt;&lt;sup&gt;3&lt;/sup&gt;&lt;/span&gt; AFMBioMed organized its first international meeting in &lt;i&gt;Barcelona&lt;/i&gt;, Spain, in spring 2007&lt;span&gt;&lt;sup&gt;4&lt;/sup&gt;&lt;/span&gt; and this was followed, at 18-month intervals, by &lt;i&gt;Monterey&lt;/i&gt;, CA, USA, in fall 2008,&lt;span&gt;&lt;sup&gt;5&lt;/sup&gt;&lt;/span&gt; &lt;i&gt;Crveni otok&lt;/i&gt; (Red Island) near the Adriatic City of Rovinj, Croatia, in spring 2010,&lt;span&gt;&lt;sup&gt;6&lt;/sup&gt;&lt;/span&gt; &lt;i&gt;Paris&lt;/i&gt; in summer 2011,&lt;span&gt;&lt;sup&gt;7&lt;/sup&gt;&lt;/span&gt; &lt;i&gt;Shanghai&lt;/i&gt; in spring 2013,&lt;span&gt;&lt;sup&gt;8&lt;/sup&gt;&lt;/span&gt; &lt;i&gt;San Diego&lt;/i&gt; in fall 2014,&lt;span&gt;&lt;sup&gt;9&lt;/sup&gt;&lt;/span&gt; &lt;i&gt;Porto&lt;/i&gt; in spring 2016,&lt;span&gt;&lt;sup&gt;10&lt;/sup&gt;&lt;/span&gt; &lt;i&gt;Krakow&lt;/i&gt; in fall 2017,&lt;span&gt;&lt;sup&gt;3&lt;/sup&gt;&lt;/span&gt; and &lt;i&gt;Münster&lt;/i&gt; in fall 2019.&lt;span&gt;&lt;sup&gt;11&lt;/sup&gt;&lt;/span&gt;&lt;/p&gt;&lt;p&gt;Members of the scientific committee for the tenth edition of the AFMBioMed meeting in Nagoya-Okasaki, Japan, in summer 2022 include past and present organizers &lt;i&gt;Takayuki Uchihashi&lt;/i&gt; (Nagoya University, Japan), &lt;i&gt;Hermann Schillers&lt;/i&gt; (University of Münster, Germany), &lt;i&gt;Malgorzata Lekka&lt;/i&gt; (Polish Academy of Sciences, Poland), &lt;i&gt;Susana R. Sousa&lt;/i&gt; (i3S|INEB, Porto, Portugal), &lt;i&gt;Adam Engler&lt;/i&gt; (UCSD, San Diego, USA), &lt;i&gt;Jun Hu&lt;/i&gt; (SINAP, Shanghai, China), &lt;i&gt;Sanjay Kumar&lt;/i&gt; (University of California, Berkeley, USA), &lt;i&gt;Daniel Navajas&lt;/i&gt; (Universitat de Barcelona, Barcelona, Spain), &lt;i&gt;Simon Scheuring&lt;/i&gt; (Institut National de la Santé et de la Recherche Médicale (INSERM) U1006, Marseille, France), &lt;i&gt;Vesna Svetlicic&lt;/i&gt; (Rudjer Boskovic Institute, Zagreb, Croatia), the original founders of the conference &lt;i&gt;Pierre Parot&lt;/i&gt; (IACA) and &lt;i&gt;Jean-Luc Pellequer&lt;/i&gt; (CEA/DRF, Institut de Biologie Structurale, Grenoble, France), as well as the four invited chairs: &lt;i&gt;Alice Pyne&lt;/i&gt; (Sheffield University, UK), &lt;i&gt;Felix Rico&lt;/i&gt; (Aix-Marseille University—INSERM, France), &lt;i&gt;Takaharu Okajima&lt;/i&gt; (Hokkaido University, Japan), and &lt;i&gt;Noriyuki Kodera&lt;/i&gt; (Kanazawa University, Japan).&lt;/p&gt;&lt;p&gt;The 10th AFMBioMed was scheduled as a landmark conference. Despite the round number 10, it was the last conference organized with a single AFM sponsor (more below). It should have been the last conference that Pierre Parot, the co-founder of AFMBioMed, would participate in. At the end of the 9th conference in Münster, the 10th AFMBioMed conference was initially planned for spring 2021, the cherry blossom season in Japan. Unfortunately, the COVID-19 pandemic modified our plan. The conference was postponed every 6 months while waiting for the reopening of travel to Japan (as well as other countries). In early 2022, the organi","PeriodicalId":16531,"journal":{"name":"Journal of Molecular Recognition","volume":"37 3","pages":""},"PeriodicalIF":2.7,"publicationDate":"2024-02-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://onlinelibrary.wiley.com/doi/epdf/10.1002/jmr.3077","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139983169","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}