Effects of p-sulfonatocalixarene and p-sulfonatocalixarene/sulfobetaine surfactant complex on the activities of bromelain and polyphenol oxidase

Xia, Shuhuai; Jiang, Yujun; Guo, Xia; Wang, Yaqiong; Xu, Wenlin

doi:10.1016/j.molliq.2022.120398

Cited by 5 publications

(4 citation statements)

References 37 publications

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“…In this case, the smallest calix [4]arene represents the ideal scaffold to develop inhibitors, due to its rigidity that strongly reduces the entropic penalty typical of every binding process. Calixarene derivatives are efficient inhibitors of alkaline phosphatase, [34][35][36] ion channels, [37] histone deacetylase, [38] galectin-1, [39,40] glutathione-S-transferase, [41,42] tyrosine phosphatase, [43][44][45][46] HIV-1 integrase, [47,48] HIV protease, [49] protein disulfide isomerase, [50] AXL tyrosine kinase receptor, [51] HIV-1 nucleocapsid protein, [52] α-mannosidase, [53] bromelain and polyphenol oxidase, [54] and carbonic anhydrase. [55] Over the last twenty years, a substantial amount of work was carried out to study the interaction of calixarene derivatives with biomolecules, in particular to identify their interactions with druggable proteins.…”

Section: Introductionmentioning

confidence: 99%

Identification of Potential Drug Targets of Calix[4]arene by Reverse Docking

Giugliano,

Gajo,

Marforio

et al. 2024

Chemistry A European J

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Calixarenes are displaying great potential for the development of new drug delivery systems, diagnostic imaging, biosensing devices and inhibitors of biological processes. In particular, calixarene derivatives are able to interact with many different enzymes and function as inhibitors. By screening of the potential drug target database (PDTD) with a reverse docking procedure, we identify and discuss a selection of 100 proteins that interact strongly with calix[4]arene. We also discover that leucine (23.5%), isoleucine (11.3%), phenylalanines (11.3%) and valine (9.5%) are the most frequent binding residues followed by hydrophobic cysteines and methionines and aromatic histidines, tyrosines and tryptophanes. Top binders are peroxisome proliferator‐activated receptors that already are targeted by commercial drugs, demonstrating the practical interest in calix[4]arene. Nuclear receptors, potassium channel, several carrier proteins, a variety of cancer‐related proteins and viral proteins are prominent in the list. It is concluded that calix[4]arene, which is characterized by facile access, well‐defined conformational characteristics, and ease of functionalization at both the lower and higher rims, could be a potential lead compound for the development of enzyme inhibitors and theranostic platforms.

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Section: Introductionmentioning

confidence: 99%

Identification of Potential Drug Targets of Calix[4]arene by Reverse Docking

Giugliano,

Gajo,

Marforio

et al. 2024

Chemistry A European J

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“…Calixarenes, due to their tunable size up to giant calixarenes 14 and to their large possibilities of functionalization, 15,16 are associated with many applications in biological fields, as chemotherapy delivery carriers, 17,18 protein inhibitors 19,20 and surface binders-recognizers. 21,22 The specific interaction with overall positively-charged proteins, like cytochrome-C, 6,23 lysozyme 24 and small antifungal proteins (PAF), 25,26 makes calixarenes ideal ligand host partners 27 in encapsulating positivelycharged residues such as lysines and arginines, 28 as their binding is governed by electrostatic interactions.…”

Section: Introductionmentioning

confidence: 99%

“…1A. It consists in unbiased, diffusion MD simulations with many independent replica (20), followed by ''Bound-state'' and free energy MD simulations, based on the Attach-Pull-Release (APR) [33][34][35] method, to: (i) assign de novo plausible competitive binding sites, independently from the crystallographic ones, (ii) estimate the free energy of binding to be compared to ITC measurements and (iii) characterize the dynamics of binding and possible structural consequences on competitive salt bridges.…”

Section: Introductionmentioning

confidence: 99%

Probing the dynamical interaction of the para-sulfonato-calix[4]arene with an antifungal protein

Bartocci¹,

Dumont²

2023

Phys. Chem. Chem. Phys.

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“…Calixarenes, due to their tunable size up to giant calixarenes 16 and to their large possibilities of functionalization [17][18][19][20][21] , are associated with many applications in biological fields, as chemotherapy delivery carriers [22][23][24][25][26][27] , protein inhibitors 28,29 and surface binders-recognizers 15,[30][31][32] .…”

Section: Introductionmentioning

confidence: 99%

Probing the dynamical interaction of the para-sulfonato-calix[4]arene with an antifungal protein

Bartocci

Dumont

2023

Preprint

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Calixarenes are hallmark molecules in supramolecular chemistry as guest cages for small ligands. They have also conversely proved their interest as auxiliary ligands toward assisted co-crystallization of proteins. These functionalized macromolecular cages target positively-charges residues, and notably surface-exposed lysines, with a site-selectivity finely characterized experimentally, but that remains to be assessed. Relying on a tailored molecular dynamics simulations protocol, we explore the association of para-sulfonato-calix[4]arenes with an antifungal protein, as a small yet most competitive system with 13 surface-exposed lysines. Our computational approach probe "de novo" the electrostatically-driven interaction, ruled out by a competition with salt bridges, not only corroborating the main binding site probed by X-ray, but also characterizing a second binding site that can act as a transient hub spot. The attach-pull-release (APR) method provides a very good assessment of the overall binding free energy measured experimentally (-6.42+-0.5 vs -5.45 kcal.mol-1 by isothermal titration calorimetry). This work also probes dynamical allosteric modifications upon ligand binding, and our computational protocol could be generalized to situate the supramolecular forces ruling out the calixarene-assisted co-crystallization of proteins.

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Effects of p-sulfonatocalixarene and p-sulfonatocalixarene/sulfobetaine surfactant complex on the activities of bromelain and polyphenol oxidase

Cited by 5 publications

References 37 publications

Identification of Potential Drug Targets of Calix[4]arene by Reverse Docking

Identification of Potential Drug Targets of Calix[4]arene by Reverse Docking

Probing the dynamical interaction of the para-sulfonato-calix[4]arene with an antifungal protein

Probing the dynamical interaction of the para-sulfonato-calix[4]arene with an antifungal protein

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