{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2025,12,2]],"date-time":"2025-12-02T15:15:03Z","timestamp":1764688503623,"version":"3.46.0"},"reference-count":55,"publisher":"MDPI AG","issue":"23","license":[{"start":{"date-parts":[[2025,12,2]],"date-time":"2025-12-02T00:00:00Z","timestamp":1764633600000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"funder":[{"DOI":"10.13039\/501100004442","name":"National Science Centre, Poland","doi-asserted-by":"publisher","award":["N N204 355540"],"award-info":[{"award-number":["N N204 355540"]}],"id":[{"id":"10.13039\/501100004442","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["IJMS"],"abstract":"<jats:p>Nucleopeptides (NPs) are unnatural hybrid polymers designed by coupling nucleobases to the side chains of amino acid residues within peptides. In this study, we present the synthesis of an Fmoc-protected nucleobase amino acid (NBA) monomer (Fmoc-1,4-TzlNBAA) with adenine attached to the side chain of L-homoazidoalanine (Aha) through a 1,4-linked-1,2,3-triazole. The coupling was accomplished by a Cu(I)-catalyzed azide\u2013alkyne cycloaddition (CuAAC) of Fmoc-Aha and N9-propargyladenine. Subsequently, a homotrinucleopeptide (HalTzlAAA) containing three 1,4-TzlNBAA residues was synthesized, using different solid-phase peptide synthesis (SPPS) approaches, and its ability to recognize U-rich motifs of RNAs involved in the HIV replication cycle was studied using circular dichroism (CD) and fluorescence spectroscopy. CD curves confirmed the binding of HalTzlAAA to U-rich motifs of the transactivation responsive element (TAR UUU RNA HIV-1) bulge and the anticodon stem\u2013loop domain of human tRNALys3 (ASLLys3) by a decrease in the positive ellipticity band intensity around 265 nm during the complexation. 5\u2032-(FAM(6))-labeled TAR UUU and hASLLys3 were used for fluorescence anisotropy binding studies. Fluorescence data revealed that HalTzlAAA bound TAR\u2019s UUU bulge with a moderate affinity (Kd \u2248 38 \u00b5M), whereas the ASLLys3 UUUU-containing loop sequence was recognized with 2.5 times lower affinity (with Kd \u2248 75 \u00b5M). Both the standard SPPS method and its variants, which involved the attachment of adenine to the L-Aha side chain using the click reaction during the synthesis on the resin or after the nucleopeptide cleavage, were characterized by a similar efficiency and yield. The CD and fluorescence results demonstrated that HalTzlAAA recognized the U-rich sequences of the RNAs with moderate and varied affinities. It is likely that both the hydrogen bonds associated with the complementarity of the interacting sequences and the conformational aspects associated with the high conformational dynamics of U-rich motifs are important in the recognition process. The nucleopeptide represents a new class of RNA binders and may be a promising scaffold for the development of new antiviral drugs.<\/jats:p>","DOI":"10.3390\/ijms262311687","type":"journal-article","created":{"date-parts":[[2025,12,2]],"date-time":"2025-12-02T15:03:13Z","timestamp":1764687793000},"page":"11687","update-policy":"https:\/\/doi.org\/10.3390\/mdpi_crossmark_policy","source":"Crossref","is-referenced-by-count":0,"title":["Solid-Phase Synthesis Approaches and U-Rich RNA-Binding Activity of Homotrimer Nucleopeptide Containing Adenine Linked to L-azidohomoalanine Side Chain via 1,4-Linked-1,2,3-Triazole"],"prefix":"10.3390","volume":"26","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-0269-8620","authenticated-orcid":false,"given":"Piotr","family":"Mucha","sequence":"first","affiliation":[{"name":"Laboratory of Biologically Active Compounds Chemistry, Department of Molecular Biochemistry, Faculty of Chemistry, University of Gdansk, Wita Stwosza 63, 80-308 Gdansk, Poland"},{"name":"Environmental Nucleic Acid Laboratory, Faculty of Chemistry, University of Gdansk, Wita Stwosza 63, 80-308 Gdansk, Poland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Ma\u0142gorzata","family":"Pieszko","sequence":"additional","affiliation":[{"name":"Laboratory of Biologically Active Compounds Chemistry, Department of Molecular Biochemistry, Faculty of Chemistry, University of Gdansk, Wita Stwosza 63, 80-308 Gdansk, Poland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Irena","family":"Byli\u0144ska","sequence":"additional","affiliation":[{"name":"Laboratory of Photobiophysics, Department of Biomedical Chemistry, Faculty of Chemistry, University of Gdansk, Wita Stwosza 63, 80-308 Gdansk, Poland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-3278-5514","authenticated-orcid":false,"given":"Wies\u0142aw","family":"Wiczk","sequence":"additional","affiliation":[{"name":"Laboratory of Photobiophysics, Department of Biomedical Chemistry, Faculty of Chemistry, University of Gdansk, Wita Stwosza 63, 80-308 Gdansk, Poland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1945-194X","authenticated-orcid":false,"given":"Jaros\u0142aw","family":"Ruczy\u0144ski","sequence":"additional","affiliation":[{"name":"Laboratory of Biologically Active Compounds Chemistry, Department of Molecular Biochemistry, Faculty of Chemistry, University of Gdansk, Wita Stwosza 63, 80-308 Gdansk, Poland"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-6994-4833","authenticated-orcid":false,"given":"Piotr","family":"Rekowski","sequence":"additional","affiliation":[{"name":"Laboratory of Biologically Active Compounds Chemistry, Department of Molecular Biochemistry, Faculty of Chemistry, University of Gdansk, Wita Stwosza 63, 80-308 Gdansk, Poland"},{"name":"Environmental Nucleic Acid Laboratory, Faculty of Chemistry, University of Gdansk, Wita Stwosza 63, 80-308 Gdansk, Poland"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"1968","published-online":{"date-parts":[[2025,12,2]]},"reference":[{"key":"ref_1","doi-asserted-by":"crossref","unstructured":"Harries, L.W. (2019). RNA Biology Provides New Therapeutic Targets for Human Disease. Front. Genet., 10.","DOI":"10.3389\/fgene.2019.00205"},{"key":"ref_2","doi-asserted-by":"crossref","first-page":"1","DOI":"10.14348\/molcells.2023.0010","article-title":"RNA in Biology and Therapeutics","volume":"46","author":"Jeong","year":"2023","journal-title":"Mol. Cells"},{"key":"ref_3","doi-asserted-by":"crossref","first-page":"644","DOI":"10.1038\/s41419-022-05075-2","article-title":"RNA-based therapeutics: An overview and prospectus","volume":"13","author":"Zhu","year":"2022","journal-title":"Cell Death Dis."},{"key":"ref_4","doi-asserted-by":"crossref","unstructured":"Damase, T.R., Sukhovershin, R., Boada, C., Taraballi, F., Pettigrew, R.I., and Cooke, J.P. (2021). The Limitless Future of RNA Therapeutics. Front. Bioeng. Biotechnol., 9.","DOI":"10.3389\/fbioe.2021.628137"},{"key":"ref_5","doi-asserted-by":"crossref","first-page":"14191","DOI":"10.1021\/bi010978o","article-title":"Anticodon domain methylated nucleosides of yeast tRNA(Phe) are significant recognition determinants in the binding of a phage display selected peptide","volume":"40","author":"Mucha","year":"2001","journal-title":"Biochemistry"},{"key":"ref_6","doi-asserted-by":"crossref","unstructured":"Singh, G., and Monga, V. (2023). Peptide Nucleic Acids: Recent Developments in the Synthesis and Backbone Modifications. Bioorg. Chem., 141.","DOI":"10.1016\/j.bioorg.2023.106860"},{"key":"ref_7","doi-asserted-by":"crossref","unstructured":"Wang, F., Li, P., Chu, H.C., and Lo, P.K. (2022). Nucleic Acids and Their Analogues for Biomedical Applications. Biosensors, 12.","DOI":"10.3390\/bios12020093"},{"key":"ref_8","doi-asserted-by":"crossref","first-page":"736","DOI":"10.1038\/s41573-022-00521-4","article-title":"Targeting RNA structures with small molecules","volume":"21","author":"Yang","year":"2022","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_9","doi-asserted-by":"crossref","first-page":"547","DOI":"10.1038\/nrd.2018.93","article-title":"Principles for targeting RNA with drug-like small molecules","volume":"17","author":"Warner","year":"2018","journal-title":"Nat. Rev. Drug Discov."},{"key":"ref_10","doi-asserted-by":"crossref","first-page":"20160116","DOI":"10.1098\/rsfs.2016.0116","article-title":"Self-assembly of nucleopeptides to interact with DNAs","volume":"7","author":"Du","year":"2017","journal-title":"Interface Focus"},{"key":"ref_11","doi-asserted-by":"crossref","unstructured":"Mucha, P., Pieszko, M., Byli\u0144ska, I., Wiczk, W., Ruczy\u0144ski, J., Prochera, K., and Rekowski, P. (2024). Solid Phase Synthesis and TAR RNA-Binding Activity of Nucleopeptides Containing Nucleobases Linked to the Side Chains via 1,4-Linked-1,2,3-triazole. Biomedicines, 12.","DOI":"10.3390\/biomedicines12030570"},{"key":"ref_12","doi-asserted-by":"crossref","first-page":"2613","DOI":"10.2147\/IJN.S156381","article-title":"DNA- and RNA-binding ability of oligoDapT, a nucleobase-decorated peptide, for biomedical applications","volume":"13","author":"Musumeci","year":"2018","journal-title":"Int. J. Nanomed."},{"key":"ref_13","doi-asserted-by":"crossref","first-page":"11612","DOI":"10.1021\/acs.joc.6b01829","article-title":"Switchable Protecting Strategy for Solid Phase Synthesis of DNA and RNA Interacting Nucleopeptides","volume":"81","author":"Mercurio","year":"2016","journal-title":"J. Org. Chem."},{"key":"ref_14","doi-asserted-by":"crossref","first-page":"8093","DOI":"10.1039\/c2cc33477a","article-title":"Fully automated sequential solid phase approach towards viral RNA-nucleopeptides","volume":"48","author":"Meeuwenoord","year":"2012","journal-title":"Chem. Commun."},{"key":"ref_15","doi-asserted-by":"crossref","unstructured":"Verona, M., Verdolino, V., Palazzesi, F., and Corradini, R. (2017). Focus on PNA Flexibility and RNA Binding using Molecular Dynamics and Metadynamics. Sci. Rep., 7.","DOI":"10.1038\/srep42799"},{"key":"ref_16","doi-asserted-by":"crossref","first-page":"694","DOI":"10.1038\/sj.ejhg.5201226","article-title":"The peptide nucleic acids (PNAs), powerful tools for molecular genetics and cytogenetics","volume":"12","author":"Pellestor","year":"2004","journal-title":"Eur. J. Hum. Genet."},{"key":"ref_17","doi-asserted-by":"crossref","first-page":"1937","DOI":"10.1093\/nar\/gkv1513","article-title":"The first crystal structures of RNA-PNA duplexes and a PNA-PNA duplex containing mismatches\u2014Toward anti-sense therapy against TREDs","volume":"44","author":"Kiliszek","year":"2016","journal-title":"Nucleic Acids Res."},{"key":"ref_18","first-page":"583","article-title":"Therapeutic Peptide Nucleic Acids: Principles, Limitations, and Opportunities","volume":"90","author":"Quijano","year":"2017","journal-title":"Yale J. Biol. Med."},{"key":"ref_19","doi-asserted-by":"crossref","first-page":"102086","DOI":"10.1016\/j.omtn.2023.102086","article-title":"Therapeutic and diagnostic applications of antisense peptide nucleic acids","volume":"35","author":"MacLelland","year":"2023","journal-title":"Mol. Ther. Nucleic Acids"},{"key":"ref_20","doi-asserted-by":"crossref","unstructured":"Musumeci, D., Mokhir, A., and Roviello, G.N. (2020). Synthesis and nucleic acid binding evaluation of a thyminyl l-diaminobutanoic acid-based nucleopeptide. Bioorg. Chem., 100.","DOI":"10.1016\/j.bioorg.2020.103862"},{"key":"ref_21","doi-asserted-by":"crossref","first-page":"63578","DOI":"10.1039\/C6RA08765E","article-title":"Synthetic approaches to nucleopeptides containing all four nucleobases, and nucleic acid-binding studies on a mixed-sequence nucleo-oligolysine","volume":"6","author":"Roviello","year":"2016","journal-title":"RSC Adv."},{"key":"ref_22","doi-asserted-by":"crossref","first-page":"14140","DOI":"10.1039\/C5RA25809J","article-title":"Solid phase synthesis and RNA-binding activity of an arginine-containing nucleopeptide","volume":"6","author":"Roviello","year":"2016","journal-title":"RSC Adv."},{"key":"ref_23","doi-asserted-by":"crossref","unstructured":"You, Y., Chen, C.Y., and Shyu, A.B. (1992). U-rich sequence-binding proteins (URBPs) interacting with a 20-nucleotide U-rich sequence in the 3\u2032 untranslated region of c-fos mRNA may be involved in the first step of c-fos mRNA degradation. Mol. Cell Biol., 12.","DOI":"10.1128\/MCB.12.7.2931"},{"key":"ref_24","doi-asserted-by":"crossref","first-page":"267","DOI":"10.1016\/j.sbi.2009.03.005","article-title":"Toward a structural understanding of IRES RNA function","volume":"19","author":"Filbin","year":"2009","journal-title":"Curr. Opin. Struct. Biol."},{"key":"ref_25","doi-asserted-by":"crossref","first-page":"521","DOI":"10.1016\/j.cell.2012.09.022","article-title":"TUT4\/7-mediated uridylation of pre-let-7 in miRNA processing","volume":"151","author":"Heo","year":"2012","journal-title":"Cell"},{"key":"ref_26","doi-asserted-by":"crossref","first-page":"106","DOI":"10.1016\/j.tibs.2011.11.005","article-title":"Small heat shock proteins and \u03b1-crystallins: Dynamic proteins with flexible functions","volume":"37","author":"Basha","year":"2012","journal-title":"Trends Biochem. Sci."},{"key":"ref_27","doi-asserted-by":"crossref","first-page":"2935","DOI":"10.1073\/pnas.1808696116","article-title":"Molecular basis for AU-rich element recognition and dimerization by the HuR C-terminal RRM","volume":"116","author":"Ripin","year":"2019","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_28","doi-asserted-by":"crossref","first-page":"862","DOI":"10.1124\/pr.120.019554","article-title":"RNA Drugs and RNA Targets for Small Molecules: Principles, Progress, and Challenges","volume":"72","author":"Yu","year":"2020","journal-title":"Pharmacol. Rev."},{"key":"ref_29","doi-asserted-by":"crossref","first-page":"251","DOI":"10.1021\/acsmedchemlett.3c00020","article-title":"Contemporary Progress and Opportunities in RNA-Targeted Drug Discovery","volume":"14","author":"Garner","year":"2023","journal-title":"ACS Med. Chem. Lett."},{"key":"ref_30","doi-asserted-by":"crossref","first-page":"4112","DOI":"10.2174\/1381612823666170616081736","article-title":"Recent Advances in Targeting the HIV-1 Tat\/TAR Complex","volume":"23","author":"Abulwerdi","year":"2017","journal-title":"Curr. Pharm. Des."},{"key":"ref_31","doi-asserted-by":"crossref","first-page":"9326","DOI":"10.1074\/jbc.REV119.006860","article-title":"Face-time with TAR: Portraits of an HIV-1 RNA with diverse modes of effector recognition relevant for drug discovery","volume":"294","author":"Chavali","year":"2019","journal-title":"J. Biol. Chem."},{"key":"ref_32","doi-asserted-by":"crossref","first-page":"191","DOI":"10.1016\/bs.ircmb.2017.07.011","article-title":"Transcription: Insights From the HIV-1 Promoter","volume":"335","author":"Ne","year":"2018","journal-title":"Int. Rev. Cell Mol. Biol."},{"key":"ref_33","doi-asserted-by":"crossref","first-page":"4098","DOI":"10.2174\/1381612823666170704130635","article-title":"The HIV-1 Tat Protein: Mechanism of Action and Target for HIV-1 Cure Strategies","volume":"23","author":"Rice","year":"2017","journal-title":"Curr. Pharm. Des."},{"key":"ref_34","doi-asserted-by":"crossref","first-page":"27569","DOI":"10.18632\/oncotarget.15174","article-title":"Tat is a multifunctional viral protein that modulates cellular gene expression and functions","volume":"8","author":"Clark","year":"2017","journal-title":"Oncotarget"},{"key":"ref_35","doi-asserted-by":"crossref","first-page":"12973","DOI":"10.1073\/pnas.1806438115","article-title":"Structural mechanism for HIV-1 TAR loop recognition by Tat and the super elongation complex","volume":"115","author":"Hurley","year":"2018","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"ref_36","doi-asserted-by":"crossref","unstructured":"Ronsard, L., Rai, T., Rai, D., Ramachandran, V.G., and Banerjea, A.C. (2017). In silico Analyses of Subtype Specific HIV-1 Tat-TAR RNA Interaction Reveals the Structural Determinants for Viral Activity. Front. Microbiol., 8.","DOI":"10.3389\/fmicb.2017.01467"},{"key":"ref_37","doi-asserted-by":"crossref","first-page":"211","DOI":"10.1016\/S0021-9673(02)00952-4","article-title":"Structural requirements for conserved Arg52 residue for interaction of the human immunodeficiency virus type 1 trans-activation responsive element with trans-activator of transcription protein (49-57). Capillary electrophoresis mobility shift assay","volume":"968","author":"Mucha","year":"2002","journal-title":"J. Chromatogr. A"},{"key":"ref_38","doi-asserted-by":"crossref","first-page":"107","DOI":"10.1080\/15216540211469","article-title":"tRNA(Lys3): The primer tRNA for reverse transcription in HIV-1","volume":"53","author":"Kleiman","year":"2002","journal-title":"IUBMB Life"},{"key":"ref_39","doi-asserted-by":"crossref","first-page":"340","DOI":"10.1016\/j.virusres.2012.06.001","article-title":"Aspects of HIV-1 assembly that promote primer tRNA(Lys3) annealing to viral RNA","volume":"169","author":"Saadatmand","year":"2012","journal-title":"Virus Res."},{"key":"ref_40","doi-asserted-by":"crossref","first-page":"698","DOI":"10.1016\/j.jmb.2011.04.025","article-title":"Functional recognition of the modified human tRNALys3(UUU) anticodon domain by HIV\u2019s nucleocapsid protein and a peptide mimic","volume":"410","author":"Graham","year":"2011","journal-title":"J. Mol. Biol."},{"key":"ref_41","doi-asserted-by":"crossref","first-page":"23867","DOI":"10.1074\/jbc.270.40.23867","article-title":"Structural requirements for the binding of tRNA Lys3 to reverse transcriptase of the human immunodeficiency virus type 1","volume":"270","author":"Das","year":"1995","journal-title":"J. Biol. Chem."},{"key":"ref_42","doi-asserted-by":"crossref","first-page":"219","DOI":"10.1261\/rna.036681.112","article-title":"Molecular mimicry of human tRNALys anti-codon domain by HIV-1 RNA genome facilitates tRNA primer annealing","volume":"19","author":"Jones","year":"2013","journal-title":"RNA"},{"key":"ref_43","doi-asserted-by":"crossref","first-page":"16470","DOI":"10.1074\/jbc.RA120.015444","article-title":"Co-crystal structures of HIV TAR RNA bound to lab-evolved proteins show key roles for arginine relevant to the design of cyclic peptide TAR inhibitors","volume":"295","author":"Chavali","year":"2020","journal-title":"J. Biol. Chem."},{"key":"ref_44","doi-asserted-by":"crossref","unstructured":"Chavali, S.S., Mali, S.M., Bonn, R., Saseendran Anitha, A., Bennett, R.P., Smith, H.C., Fasan, R., and Wedekind, J.E. (2021). Cyclic peptides with a distinct arginine-fork motif recognize the HIV trans-activation response RNA in vitro and in cells. J. Biol. Chem., 297.","DOI":"10.1016\/j.jbc.2021.101390"},{"key":"ref_45","doi-asserted-by":"crossref","first-page":"3881","DOI":"10.1128\/JVI.76.8.3881-3891.2002","article-title":"Anti-TAR polyamide nucleotide analog conjugated with a membrane-permeating peptide inhibits human immunodeficiency virus type 1 production","volume":"76","author":"Kaushik","year":"2002","journal-title":"J. Virol."},{"key":"ref_46","doi-asserted-by":"crossref","first-page":"418","DOI":"10.1016\/j.virol.2004.10.032","article-title":"A PNA-transportan conjugate targeted to the TAR region of the HIV-1 genome exhibits both antiviral and virucidal properties","volume":"331","author":"Chaubey","year":"2005","journal-title":"Virology"},{"key":"ref_47","doi-asserted-by":"crossref","first-page":"779","DOI":"10.1080\/17460441.2019.1614910","article-title":"Recent applications of click chemistry in drug discovery","volume":"14","author":"Jiang","year":"2019","journal-title":"Expert Opin. Drug Discov."},{"key":"ref_48","doi-asserted-by":"crossref","first-page":"696","DOI":"10.1002\/psc.2653","article-title":"\u2018Click\u2019 chemistry synthesis and capillary electrophoresis study of 1,4-linked 1,2,3-triazole AZT-systemin conjugate","volume":"20","author":"Dobkowski","year":"2014","journal-title":"J. Pept. Sci."},{"key":"ref_49","doi-asserted-by":"crossref","first-page":"2022","DOI":"10.2174\/0929867322666150421110819","article-title":"Click chemistry, a potent tool in medicinal sciences","volume":"22","author":"Musumeci","year":"2015","journal-title":"Curr. Med. Chem."},{"key":"ref_50","doi-asserted-by":"crossref","first-page":"2550","DOI":"10.1261\/rna.1004108","article-title":"Thermodynamic examination of trinucleotide bulged RNA in the context of HIV-1 TAR RNA","volume":"14","author":"Booth","year":"2008","journal-title":"RNA"},{"key":"ref_51","doi-asserted-by":"crossref","first-page":"116037","DOI":"10.1016\/j.ejmech.2023.116037","article-title":"Click chemistry-aided drug discovery: A retrospective and prospective outlook","volume":"264","author":"Zhao","year":"2024","journal-title":"Eur. J. Med. Chem."},{"key":"ref_52","doi-asserted-by":"crossref","first-page":"44437","DOI":"10.1021\/acsomega.3c04960","article-title":"\u201cClick Chemistry\u201d: An Emerging Tool for Developing a New Class of Structural Motifs against Various Neurodegenerative Disorders","volume":"8","author":"Manoharan","year":"2023","journal-title":"ACS Omega"},{"key":"ref_53","doi-asserted-by":"crossref","first-page":"1455","DOI":"10.1021\/acs.bioconjchem.1c00247","article-title":"An Overview of Recent Advances in Biomedical Applications of Click Chemistry","volume":"32","author":"Kaur","year":"2021","journal-title":"Bioconjug. Chem."},{"key":"ref_54","doi-asserted-by":"crossref","first-page":"9592","DOI":"10.1021\/acs.joc.5b01577","article-title":"Increasing the Stability of DNA\/RNA Duplexes by Introducing Stacking Phenyl-Substituted Pyrazole, Furan, and Triazole Moieties in the Major Groove","volume":"80","author":"Hornum","year":"2015","journal-title":"J. Org. Chem."},{"key":"ref_55","doi-asserted-by":"crossref","first-page":"2854","DOI":"10.1021\/jo4025896","article-title":"High-affinity RNA targeting by oligonucleotides displaying aromatic stacking and amino groups in the major groove. Comparison of triazoles and phenyl substituents","volume":"79","author":"Kumar","year":"2014","journal-title":"J. Org. Chem."}],"container-title":["International Journal of Molecular Sciences"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.mdpi.com\/1422-0067\/26\/23\/11687\/pdf","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,12,2]],"date-time":"2025-12-02T15:04:21Z","timestamp":1764687861000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.mdpi.com\/1422-0067\/26\/23\/11687"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,12,2]]},"references-count":55,"journal-issue":{"issue":"23","published-online":{"date-parts":[[2025,12]]}},"alternative-id":["ijms262311687"],"URL":"https:\/\/doi.org\/10.3390\/ijms262311687","relation":{},"ISSN":["1422-0067"],"issn-type":[{"value":"1422-0067","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,12,2]]}}}