Biophysical chemistry最新文献

{"title":"Decoding SARS-CoV-2 variants: Mutations, viral stability, and breakthroughs in vaccines and therapies","authors":"Zainularifeen Abduljaleel","doi":"10.1016/j.bpc.2025.107413","DOIUrl":"10.1016/j.bpc.2025.107413","url":null,"abstract":"<div><div>This study investigates the infectivity of SARS-CoV-2 and its immune evasion mechanisms, particularly through mutations in the spike protein that enable the virus to escape host immune responses. As global vaccination efforts continue, understanding viral evolution and immune evasion strategies remains critical. This analysis focuses on fourteen key mutations (Arg346Lys, Lys417Asp, Leu452Glu, Leu452Arg, Phe456Leu, Ser477Asp, Thr478Lys, Glu484Ala, Glu484Lys, Glu484Gln, Gln493Arg, Gly496Ser, Glu498Arg, and His655Y) within the receptor-binding domain (RBD) of the spike protein. The results reveal consistent patterns of immune escape across various SARS-CoV-2 variants, with specific mutations influencing protein stability, binding affinity to the hACE2 receptor, and antibody recognition. These findings demonstrate how single-point mutations can destabilize the spike protein and reduce the efficacy of the immune response. By correlating expression levels and thermodynamic stability with immune evasion, this study provides valuable insights into the functional characteristics of the spike protein. The findings contribute to the understanding of immune escape variants and identify potential targets for enhancing vaccine efficacy and developing therapeutic approaches in response to the evolving SARS-CoV-2 landscape.</div></div><div><h3>Short summary</h3><div>The study investigates the infectivity of SARS-CoV-2 and its implications for immune evasion. It focuses on fourteen key mutations within the spike protein's Receptor-Binding Domain (S-RBD) and reveals consistent patterns associated with immune escape in various SARS-CoV-2 variants. The research highlights the influence of factors such as protein fold stability, hACE2 binding, and antibody evasion on spike protein evolution. Single-point immune escape variants alter virus stability, impacting antibody response success. The study provides valuable insights into immune escape variants and suggests avenues for enhancing vaccine efficacy. It also opens the way for novel therapeutic approaches in the context of SARS-CoV-2 variants.</div></div>","PeriodicalId":8979,"journal":{"name":"Biophysical chemistry","volume":"320 ","pages":"Article 107413"},"PeriodicalIF":3.3,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143471708","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Bilirubin nanotechnology: An innovative approach in biomedicine","authors":"Alexander S. Tatikolov ,&nbsp;Pavel G. Pronkin ,&nbsp;Ina G. Panova","doi":"10.1016/j.bpc.2025.107412","DOIUrl":"10.1016/j.bpc.2025.107412","url":null,"abstract":"<div><div>Bilirubin, a product of heme catabolism, is toxic at elevated concentrations (&gt;250–300 μM in blood serum), whereas at therapeutic concentrations (∼20–200 μM) exerts potent antioxidant, anti-inflammatory, immunomodulatory, cytoprotective and neuroprotective effects. Despite the therapeutic potential, its use in clinical practice is hampered by poor aqueous solubility, instability, and rapid metabolism. Nanotechnology overcomes these limitations and additionally imparts to bilirubin the advantages characteristic of nanopreparations: targeted action on the desired organ/tissue, increased therapeutic efficacy by delaying drug elimination from the body, improved transportation over biological barriers, the ability to combine therapeutic and diagnostic properties in a single agent. The review analyses the chemical synthesis, therapeutic mechanisms, and preclinical applications of nanosystems comprising bilirubin. In particular, nanostructures obtained by the covalent binding of bilirubin to macromolecules, bilirubin encapsulation in nanocarriers, bilirubin conjugation with metal nanoparticles and nanofunctionalization of inorganic compounds are considered; the data on the therapeutic trials of nanobilirubin are summarized. While studies on animal models and in vitro systems demonstrate improved biodistribution, reduced toxicity, and enhanced efficacy, no clinical trials to date have validated nanobilirubin formulations. Key barriers may include unresolved challenges in scalable synthesis, long-term biocompatibility, reproducible dosing of nanoformulations. Hence, further development of nanotherapeutic bilirubin agents for clinical practice is urgent.</div></div>","PeriodicalId":8979,"journal":{"name":"Biophysical chemistry","volume":"320 ","pages":"Article 107412"},"PeriodicalIF":3.3,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143429135","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Photophysical and structural aspects of poly-L-tryptophan: π−π stacking interaction with an excited state intermolecular proton transfer probe 3-Hydroxynaphthoic acid revealed by experiments and molecular simulation","authors":"Priyanka Mukherjee ,&nbsp;Titas Kumar Mukhopadhyay ,&nbsp;Sagarika Sanyal ,&nbsp;Kaushik Kundu ,&nbsp;Rina Ghosh ,&nbsp;Sudeshna Shyam Chowdhury ,&nbsp;Sanjib Ghosh","doi":"10.1016/j.bpc.2025.107416","DOIUrl":"10.1016/j.bpc.2025.107416","url":null,"abstract":"<div><div>In biophysical studies involving proteins, the involvement of the intrinsic fluorophore Tryptophan and its energy transfer/binding interactions are already well-investigated areas. Theoretical studies have also been well corroborated with experimental findings. However, in polymeric Tryptophans (specifically homopolymers), several queries still need to be addressed – their structure, the environment of each Tryptophan and the binding preferences of the latter. This necessitated some detailed investigations on the poly-L-Tryptophan system both from experimental and theoretical standpoints. In this work, we have carried out both steady-state and time-resolved fluorescence studies along with low-temperature phosphorescence (LTP) of poly-L-tryptophan, and the nature of the emitting Tryptophan (Trp) residue in the latter has been characterized based on a comparison with the emission features of the parent monomer. The very large red-shift of the (0–0) band of phosphorescence in poly-L-Tryptophan has been explained through triplet-triplet energy transfer along with the structure of the latter which has been developed by theoretical modelling. The nature of the environment of the emitting Trp residue in poly-L-Trp has been compared with several multi-Tryptophan proteins where different Trp residues exhibit optically resolved (0–0) bands. The interaction of the excited state proton transfer (ESIPT) probe 3-hydroxynaphthoic acid (3-HNA) with poly-L-Trp has also been investigated in detail using fluorescence, LTP, and classical molecular dynamics simulations.</div></div>","PeriodicalId":8979,"journal":{"name":"Biophysical chemistry","volume":"320 ","pages":"Article 107416"},"PeriodicalIF":3.3,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143474788","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"A semiempirical and machine learning approach for fragment-based structural analysis of non-hydroxamate HDAC3 inhibitors","authors":"Sk. Abdul Amin ,&nbsp;Lucia Sessa ,&nbsp;Rajdip Tarafdar ,&nbsp;Shovanlal Gayen ,&nbsp;Stefano Piotto","doi":"10.1016/j.bpc.2025.107409","DOIUrl":"10.1016/j.bpc.2025.107409","url":null,"abstract":"<div><div>Interest in HDAC3 inhibitors (HDAC3i) for pharmacological applications outside of cancer is growing. However, concerns regarding the possible mutagenicity of the commonly used hydroxamates (zinc-binding groups, ZBGs) are also increasing. Considering these concerns, non-hydroxamate ZBGs offer a promising alternative for the development of non-mutagenic HDAC3 inhibitors. Unfortunately, the quantum chemical space of non-hydroxamates has not been studied in detail. This study has three primary goals: (i) to perform semiempirical quantum chemical calculations, examining AM-1 model parameters relevant to zinc binding, (ii) to develop supervised mathematical learning models to train a diverse set of non-hydroxamate-based HDAC3i, and (iii) to apply fragment-based approaches to identify sub-structural fragments (fingerprints) that promote or hinder HDAC3 inhibitory activity through classification-based QSARs. In addition, flexible molecular docking analysis, 200 ns MD simulation, and free energy landscape (FEL) analysis further established the importance of identified fingerprints in the modulation of HDAC3 inhibitory activity. This comprehensive analysis of structural variations among non-hydroxamate HDAC3i provides valuable insights, contributing to the design of potential non-mutagenic HDAC3i.</div></div>","PeriodicalId":8979,"journal":{"name":"Biophysical chemistry","volume":"320 ","pages":"Article 107409"},"PeriodicalIF":3.3,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143436748","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Unbiased clustering of residues undergoing synchronous motions in proteins using NMR spin relaxation data","authors":"V.S. Manu ,&nbsp;Giuseppe Melacini ,&nbsp;Evgenii L. Kovrigin ,&nbsp;J. Patrick Loria ,&nbsp;Gianluigi Veglia","doi":"10.1016/j.bpc.2025.107411","DOIUrl":"10.1016/j.bpc.2025.107411","url":null,"abstract":"<div><div>Biological macromolecules are dynamic entities that transition between various conformational states, often playing a vital role in biological functions. Their inherent flexibility spans a broad range of timescales. Motions occurring within the microsecond to millisecond range are especially important, as they are integral to processes such as enzyme catalysis, folding, ligand binding, and allostery. NMR Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersion measurements are the preferred method for characterizing macromolecular motions at atomic resolution. However, it is still uncertain whether the functional motions of multiple residues in macromolecules need to be coordinated and/or synchronized within the protein matrix in order to perform the desired function. Here, we illustrate an unbiased method to analyze NMR relaxation dispersion and identify dynamic clusters of residues that fluctuate on similar timescales within proteins. The method requires relaxation dispersion data for backbone amides or side-chain methyl groups, which are globally fitted using the Bloch-McConnell equations for each pair of residues. The goodness of the pairwise fitting serves as a metric to construct two-dimensional synchronous dynamics (SyncDyn) maps, allowing us to identify residue clusters whose dynamics are influenced by ligand binding. We applied our method to the catalytic subunit of the cAMP-dependent protein kinase A (PKA<img>C) and the T17A mutant of ribonuclease A (RNAse A). The SyncDyn maps for PKA-C showed distinct clusters of residues located in critical allosteric sites. Nucleotide binding activates the movement of residues at the interface between the two lobes and also those distal to the active site. In the case of RNAse A, the SyncDyn maps show that residues fluctuating with the same time scale are interspersed in both lobes of the enzyme. Overall, our approach eliminates arbitrary manual selection of residues for dynamic clustering and objectively identifies all possible residue pairs that fluctuate synchronously, <em>i.e.</em> on the same timescale.</div></div>","PeriodicalId":8979,"journal":{"name":"Biophysical chemistry","volume":"320 ","pages":"Article 107411"},"PeriodicalIF":3.3,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143444898","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Copper(II) enhances the antibacterial activity of nitroxoline against MRSA by promoting aerobic glycolysis","authors":"Xiaoyong Huang ,&nbsp;Huiting Yang ,&nbsp;Xiaomin Ren ,&nbsp;Qianqian Li ,&nbsp;Jianzhong Wang ,&nbsp;Jia Cheng ,&nbsp;Zilong Sun","doi":"10.1016/j.bpc.2025.107419","DOIUrl":"10.1016/j.bpc.2025.107419","url":null,"abstract":"<div><div>Nitroxoline (NIT) is an FDA-approved antibiotic with numerous pharmacological properties. However, the intricate connections between its metal-chelating ability and antimicrobial efficacy remain incompletely understood. The specific interactions of NIT with different metal ions were measured via UV–vis absorption spectroscopy. Here, we found that NIT can bind to various metal ions, including Cu²⁺, Fe²⁺, Zn²⁺ and Mn²⁺. However, the antimicrobial activity of NIT against methicillin-resistant <em>Staphylococcus aureus</em> (MRSA) was significantly enhanced by the inclusion of Cu²⁺ as determined by a minimal inhibitory concentration (MIC) assay in Mueller-Hinton broth. The enhanced antibacterial effect was not influenced by the availability of oxygen. Mechanistically, Cu²⁺ promoted bacterial proliferation, increased the bacterial transmembrane electrical potential, and increased intracellular acidification. In addition, Cu²⁺ rewired bacterial metabolism, promoting the uptake of glucose with a lower level of ATP production. Pharmacological upregulation of glycolysis by VLX600 could potentiate the susceptibility of MRSA to NIT. Moreover, Cu²⁺ also significantly increased the survival rate of acutely infected larvae. These collective results underscore that the enhanced antibacterial efficacy of NIT by Cu²⁺ intricately involves aerobic glycolysis in MRSA.</div></div>","PeriodicalId":8979,"journal":{"name":"Biophysical chemistry","volume":"320 ","pages":"Article 107419"},"PeriodicalIF":3.3,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143465097","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Substitutions at rheostat position 52 of LacI have long-range effects on the LacI conformational landscape","authors":"Nilusha L. Kariyawasam ,&nbsp;Anastasiia Sivchenko ,&nbsp;Liskin Swint-Kruse ,&nbsp;Paul E. Smith","doi":"10.1016/j.bpc.2025.107414","DOIUrl":"10.1016/j.bpc.2025.107414","url":null,"abstract":"<div><div>In proteins, amino acid changes at “rheostat” positions exhibit functional changes that vary with the substitution chosen: some substitutions enhance function, some are like wild-type, some are partially detrimental, while others abolish function. One way that substitutions might exert their complex effects is by altering protein conformational landscapes. To test this, we studied five substitutions of V52 in <em>E. coli</em> LacI, an experimentally-known rheostat position. For each variant, we mapped the accessible conformational landscapes by performing molecular dynamics simulations at ambient conditions and under three perturbations: increased pressure, binding to allosteric ligand “ONPF”, and ONPF plus pressure. The simulated DNA binding domain landscapes were compared to published experimentally-measured parameters, and the results suggest that complex combinations of dynamic parameters and/or additional simulations in the presence of DNA are needed to predict DNA binding specificity. For the variants regulatory domains all landscapes displayed boundaries similar to wild-type, but changes within the boundaries were unique. Of these, V52A/ONPF was striking: The regulatory domains for ONPF-bound, wild-type LacI are in an “Open” conformation and, experimentally, ONPF enhances DNA binding. Four variants responded to ONPF like wild-type, but ONPF binding to V52A shifted these domains to a “Closed” conformation that is associated with diminished DNA binding for wild-type LacI. This finding predicted that ONPF's allosteric regulation of V52A would change from “anti-inducer” to “inducer”, which we experimentally validated <em>in vivo</em> and <em>in vitro</em>. This supports the hypothesis that substituting rheostat positions can alter function by altering the relative populations on protein conformational landscapes.</div></div>","PeriodicalId":8979,"journal":{"name":"Biophysical chemistry","volume":"320 ","pages":"Article 107414"},"PeriodicalIF":3.3,"publicationDate":"2025-05-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143465098","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Mapping conformational landscape in protein folding: Benchmarking dimensionality reduction and clustering techniques on the Trp-Cage mini-protein","authors":"Sayari Bhattacharya,&nbsp;Suman Chakrabarty","doi":"10.1016/j.bpc.2025.107389","DOIUrl":"10.1016/j.bpc.2025.107389","url":null,"abstract":"<div><div>Quantitative characterization of protein conformational landscapes is a computationally challenging task due to their high dimensionality and inherent complexity. In this study, we systematically benchmark several widely used dimensionality reduction and clustering methods to analyze the conformational states of the Trp-Cage mini-protein, a model system with well-documented folding dynamics. Dimensionality reduction techniques, including Principal Component Analysis (PCA), Time-lagged Independent Component Analysis (TICA), and Variational Autoencoders (VAE), were employed to project the high-dimensional free energy landscape onto 2D spaces for visualization. Additionally, clustering methods such as K-means, hierarchical clustering, HDBSCAN, and Gaussian Mixture Models (GMM) were used to identify discrete conformational states directly in the high-dimensional space. Our findings reveal that density-based clustering approaches, particularly HDBSCAN, provide physically meaningful representations of free energy minima. While highlighting the strengths and limitations of each method, our study underscores that no single technique is universally optimal for capturing the complex folding pathways, emphasizing the necessity for careful selection and interpretation of computational methods in biomolecular simulations. These insights will contribute to refining the available tools for analyzing protein conformational landscapes, enabling a deeper understanding of folding mechanisms and intermediate states.</div></div>","PeriodicalId":8979,"journal":{"name":"Biophysical chemistry","volume":"319 ","pages":"Article 107389"},"PeriodicalIF":3.3,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143036684","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Discovery of the potential of cholesterol-lowering human CYP7 enzymes as biocatalysts for the production of C7 hydroxylated steroids","authors":"Yaraslau Dzichenka ,&nbsp;Michail Shapira ,&nbsp;Antos Sachanka ,&nbsp;Tatsiana Cherkesova ,&nbsp;Veronika Shchur ,&nbsp;Ljubica Grbović ,&nbsp;Ksenija Pavlović ,&nbsp;Bojana Vasiljević ,&nbsp;Marina Savić ,&nbsp;Andrea Nikolić ,&nbsp;Aleksandar Oklješa ,&nbsp;Jovana Ajduković ,&nbsp;Ivana Kuzminac ,&nbsp;Aliaksei Yantsevich ,&nbsp;Sergey Usanov ,&nbsp;Suzana Jovanović-Šanta","doi":"10.1016/j.bpc.2025.107393","DOIUrl":"10.1016/j.bpc.2025.107393","url":null,"abstract":"<div><div>Steroidal C7 alcohols and their esters are perspective agents in drug discovery. In addition, hydroxylation at C7 position could allow further modification of steroidal moiety. Such transformation is performed easily by the enzymes. Human steroid 7α-hydroxylases CYP7A1 and CYP7B1 are key enzymes taking part in the biotransformation of cholestanes, androstanes, pregnanes. In the article, we are focusing on the results of <em>in vitro</em> screening of a library of modified steroids toward CYP7 enzymes. A couple of compounds were found to express the affinity for binding to the enzymes, comparable with corresponding values for CYP7 natural ligands. Among them are 17-substituted androstane derivatives with N-containing pyridine ring and enone derivative of lithocholic acid, which bound by human CYP7A1, and D-seco and C16 oxime androstanes, which were identified as novel CYP7B1 ligands. Screening results revealed that both enzymes bind with high affinity a well-known drug abiraterone: in the case of CYP7A1 substrate-like binding mode was detected, with the formation of monohydroxylated product, while in case of CYP7B1 inhibitor-like binding was observed. Since CYP7 enzymes convert some of the studied compounds into their 7-hydroxy derivatives, potential of these enzymes as perspective regio- and stereoselective biocatalysts for obtaining C7 hydroxylated steroids could be assumed.</div></div>","PeriodicalId":8979,"journal":{"name":"Biophysical chemistry","volume":"319 ","pages":"Article 107393"},"PeriodicalIF":3.3,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143144407","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Molecular dynamics study on clustered DNA damage: AP sites on the same strand","authors":"Kazushi Terakawa ,&nbsp;Susumu Fujiwara ,&nbsp;Tomoko Mizuguchi ,&nbsp;Hiroaki Nakamura ,&nbsp;Ken Akamatsu ,&nbsp;Naoya Shikazono ,&nbsp;Yoshiteru Yonetani","doi":"10.1016/j.bpc.2025.107394","DOIUrl":"10.1016/j.bpc.2025.107394","url":null,"abstract":"<div><div>Although radiation-induced clustered DNA damage can have critical biological consequences, the underlying molecular mechanisms remain unclear. To explore the effect of clustered DNA damage on DNA structure and dynamics, we performed molecular dynamics simulations on damaged DNA with two AP sites on the same strand, that is, a tandem AP cluster. The results showed that the cluster insertion of the two AP sites had a significant impact on the DNA's local and global structures. Local structural deformations as well as the extrahelical form, AP-base pairs, and irregular base pairs were frequently observed. Unlike a single AP site, the tandem AP cluster revealed that these local structural features occurred simultaneously within a small separation. Moreover, we found that the presence of tandem AP sites induced global bending of DNA. This suggests that the present case with tandem AP sites may have a non-negligible impact on the biological function of damage repair.</div></div>","PeriodicalId":8979,"journal":{"name":"Biophysical chemistry","volume":"319 ","pages":"Article 107394"},"PeriodicalIF":3.3,"publicationDate":"2025-04-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143073666","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}