Please use this identifier to cite or link to this item:
https://hdl.handle.net/10316/115114
DC Field | Value | Language |
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dc.contributor.author | Silva Moreira, Micaeli Louise da | - |
dc.contributor.author | Chaves, Otávio Augusto | - |
dc.contributor.author | Lucas, Nanci Camara de | - |
dc.contributor.author | Silva Goulart, Juliana da | - |
dc.contributor.author | Garden, Simon J. | - |
dc.contributor.author | Serpa, Carlos | - |
dc.contributor.author | Netto-Ferreira, José Carlos | - |
dc.date.accessioned | 2024-05-08T15:49:05Z | - |
dc.date.available | 2024-05-08T15:49:05Z | - |
dc.date.issued | 2024 | - |
dc.identifier.issn | 01677322 | pt |
dc.identifier.uri | https://hdl.handle.net/10316/115114 | - |
dc.description.abstract | The intermolecular interaction between 2-(N-phenyl-N-methyl)aminonaphtho-1,4-quinone (1) and 2-(4-N-methylaminophenyl)naphtho-1,4-quinone (2) and human serum albumin (HSA) was investigated using spectroscopic techniques combined with in silico calculations via molecular docking. Steady-state titration of HSA fluorescence by 1 and 2 (λexc 295 nm) in PBS at 305, 310, and 315 K, as well as studies employing time-resolved fluorescence emission, demonstrated that the HSA:1 and HSA:2 interaction occurs through a static quenching mechanism. The Stern-Volmer constant (Ksv) values, (1.56 ± 0.08) and (3.05 ± 0.10) × 104 L/mol at 310 K for HSA:1 and HSA:2, respectively, indicate a moderate binding affinity. Van't Hoff plots showed that HSA:1 and HSA:2 interactions are spontaneous (negative ΔGo) with a hydrophobic character (ΔSo value of 0.00707 ± 0.00106 and 0.0392 ± 0.0062 kJ/mol K for HSA:1 and HSA:2, respectively) and specific electrostatic interactions (ΔHo value of –22.7 ± 3.3 and −14.4 ± 1.9 kJ/mol for HSA:1 and HSA:2, respectively). Synchronous fluorescence results showed significant perturbation in the microenvironment of the tryptophan residue (Trp-214). Circular dichroism indicated that after interaction with naphthoquinones 1 and 2, the HSA structure remains predominantly in the α-helix form. Finally, molecular docking revealed the formation of hydrophobic, electrostatic, and hydrogen bond interactions with the surrounding amino acid residues in subdomain IIA of HSA, which contains the Trp-214 residue, validated with the experimental drug-displacement assays. Overall, spectroscopic and in silico characterization of HSA:1 and HSA:2 might reflect in a low half-life in the human bloodstream, indicating the necessity of methods to improve the bioavailability, e.g., studies on the type of administration (oral versus intravenous). | pt |
dc.language.iso | eng | pt |
dc.publisher | Elsevier | pt |
dc.relation | info:eu-repo/grantAgreement/FCT/6817 - DCRRNI ID/UIDP/00313/2020/PT | pt |
dc.relation | UIDB/00313/2020 | pt |
dc.rights | closedAccess | pt |
dc.rights.uri | http://creativecommons.org/licenses/by-nc/4.0/ | pt |
dc.subject | Human Serum Albumin | pt |
dc.subject | Molecular Docking | pt |
dc.subject | Naphtho-1,4-quinone derivatives | pt |
dc.subject | Spectroscopy | pt |
dc.title | Spectroscopic and in silico characterization of the interaction between synthetic 2-substituted-naphtho-1,4-quinones and human serum albumin | pt |
dc.type | article | - |
degois.publication.firstPage | 124829 | pt |
degois.publication.title | Journal of Molecular Liquids | pt |
dc.relation.publisherversion | https://www.sciencedirect.com/science/article/pii/S0167732224008857 | pt |
dc.peerreviewed | yes | pt |
dc.identifier.doi | 10.1016/j.molliq.2024.124829 | pt |
degois.publication.volume | 403 | pt |
dc.date.embargo | 2024-01-01 | * |
uc.date.periodoEmbargo | 0 | pt |
item.openairetype | article | - |
item.fulltext | Com Texto completo | - |
item.languageiso639-1 | en | - |
item.grantfulltext | reserved | - |
item.cerifentitytype | Publications | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
crisitem.project.grantno | Coimbra Chemistry Center | - |
crisitem.author.researchunit | CQC - Coimbra Chemistry Centre | - |
crisitem.author.researchunit | CQC - Coimbra Chemistry Centre | - |
crisitem.author.parentresearchunit | Faculty of Sciences and Technology | - |
crisitem.author.parentresearchunit | Faculty of Sciences and Technology | - |
crisitem.author.orcid | 0000-0001-6211-7659 | - |
crisitem.author.orcid | 0000-0001-7004-0110 | - |
Appears in Collections: | I&D CQC - Artigos em Revistas Internacionais |
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1-s2.0-S0167732224008857-main.pdf | 6.6 MB | Adobe PDF | Request a copy |
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