Publicaciones de Horacio Poblete
2025
Espinoza-Arcos, L. Gonzalo; González-Avendaño, Mariela; Zuñiga-Bustos, Matias; Zamora, Ricardo A.; Vergara-Jaque, Ariela; Poblete, Horacio
Exploring a peripheral PIP2-binding site and its role in the alternative regulation of the TRP channel superfamily Artículo de revista
En: 2025.
@article{nokey,
title = {Exploring a peripheral PIP2-binding site and its role in the alternative regulation of the TRP channel superfamily},
author = {L. Gonzalo Espinoza-Arcos and Mariela González-Avendaño and Matias Zuñiga-Bustos and Ricardo A. Zamora and Ariela Vergara-Jaque and Horacio Poblete},
doi = {10.1085/jgp.202413574},
year = {2025},
date = {2025-11-03},
abstract = {Phosphatidylinositol 4,5-bisphosphate (PIP2) is recognized as an essential modulator of transient receptor potential (TRP) channels. Specifically, it influences the vanilloid receptor I (TRPV1), a pain receptor activated by a wide range of stimuli, including the binding of phospholipids, such as PIP2. The primary PIP2-binding site in TRPV1 has been identified through advanced techniques, revealing that the PIP2 binds to a specific pocket composed of positively charged residues located predominantly within the proximal C-terminus region. Additionally, a conserved segment with positively charged amino acids, K431 and R432, situated at the beginning of TRPV1's S1 transmembrane domain, has attracted considerable attention from the TRP research community. To date, our knowledge of this site's function and the subsequent effects following PIP2 binding is still emerging. In this work, MD simulations were conducted using coarse-grained models to investigate the binding dynamics of PIP2 on both WT and various mutated forms of TRPV1 channels. Our findings indicate that the K431A and R432A mutations significantly reduce the frequency of PIP2 contacts, suggesting that these mutated residues are part of a "peripheral binding pocket." This pocket seems to play a crucial role in facilitating the entry of PIP2 to the TRPV1 channel's primary binding site. Furthermore, our research has shown that these highly conserved residues within the TRPV subfamily are also structurally conserved across other TRP subfamilies, such as TRPM and TRPC, a detail not evident from sequence alignment alone. Consequently, we propose the existence of a structurally conserved peripheral PIP2-binding site shared among the diverse members of the TRP family, which can be categorized into distinct subfamilies.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Phosphatidylinositol 4,5-bisphosphate (PIP2) is recognized as an essential modulator of transient receptor potential (TRP) channels. Specifically, it influences the vanilloid receptor I (TRPV1), a pain receptor activated by a wide range of stimuli, including the binding of phospholipids, such as PIP2. The primary PIP2-binding site in TRPV1 has been identified through advanced techniques, revealing that the PIP2 binds to a specific pocket composed of positively charged residues located predominantly within the proximal C-terminus region. Additionally, a conserved segment with positively charged amino acids, K431 and R432, situated at the beginning of TRPV1's S1 transmembrane domain, has attracted considerable attention from the TRP research community. To date, our knowledge of this site's function and the subsequent effects following PIP2 binding is still emerging. In this work, MD simulations were conducted using coarse-grained models to investigate the binding dynamics of PIP2 on both WT and various mutated forms of TRPV1 channels. Our findings indicate that the K431A and R432A mutations significantly reduce the frequency of PIP2 contacts, suggesting that these mutated residues are part of a "peripheral binding pocket." This pocket seems to play a crucial role in facilitating the entry of PIP2 to the TRPV1 channel's primary binding site. Furthermore, our research has shown that these highly conserved residues within the TRPV subfamily are also structurally conserved across other TRP subfamilies, such as TRPM and TRPC, a detail not evident from sequence alignment alone. Consequently, we propose the existence of a structurally conserved peripheral PIP2-binding site shared among the diverse members of the TRP family, which can be categorized into distinct subfamilies.
Navarro-Quezada, Nieves; Salas-Sepúlveda, Francisca; Poblete, Horacio; Naranjo, David
Charybdotoxin binding to Shaker K+ channels is temperature sensitive in high external K+ but not in high external Na+ Artículo de revista
En: 2025.
@article{Navarro-Quezada2025,
title = {Charybdotoxin binding to Shaker K+ channels is temperature sensitive in high external K+ but not in high external Na+},
author = {Nieves Navarro-Quezada and Francisca Salas-Sepúlveda and Horacio Poblete and David Naranjo},
doi = {10.1085/jgp.202413590},
year = {2025},
date = {2025-08-07},
urldate = {2025-08-07},
abstract = {Charybdotoxin (CTX), a peptide neurotoxin derived from the scorpion Leiurus quinquestriatus, binds to the external entrance of open voltage-gated K+ channels (VGKCs) with minimal conformational impact. By occluding the VGKC pore, CTX blocks passive K+ flow—a defining function of these membrane proteins. Due to its mechanistic simplicity and high signal-to-noise ratio, the CTX–VGKC interaction is an ideal system to investigate the molecular details of binding and unbinding. CTX bound to the Shaker VGKC exhibits thermal motion (wobbling) that permits access of external K+ to the channel pore. To test whether this wobbling is part of the reaction pathway during toxin–channel interaction, the energetic role of external K+ was examined in the association and dissociation kinetics. A high-affinity Shaker K427E-VGKC variant was expressed in Xenopus oocytes, and its activity was monitored via two-electrode voltage clamp between ∼10 and ∼30°C. Nanomolar applications of CTX to open and closed channels, in the presence of high external Na+ or high K+ concentrations, were used to measure blockade kinetics at different voltages and temperatures. In high K+, both the dissociation and association rates showed higher activation enthalpies, by ∼15 kJ/mol and ∼25 kJ/mol, respectively, compared with high Na+ conditions. However, the association rates under high Na+ and K+ were equal at ∼20°C, indicating a compensatory K+-induced activation entropy. We propose transient CTX-wobbling intermediates in both directions of the reaction pathway. Such a wobbling intermediate could enhance the diversity of productive collisions during association, increasing the efficacy of the scorpion venom.
},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Charybdotoxin (CTX), a peptide neurotoxin derived from the scorpion Leiurus quinquestriatus, binds to the external entrance of open voltage-gated K+ channels (VGKCs) with minimal conformational impact. By occluding the VGKC pore, CTX blocks passive K+ flow—a defining function of these membrane proteins. Due to its mechanistic simplicity and high signal-to-noise ratio, the CTX–VGKC interaction is an ideal system to investigate the molecular details of binding and unbinding. CTX bound to the Shaker VGKC exhibits thermal motion (wobbling) that permits access of external K+ to the channel pore. To test whether this wobbling is part of the reaction pathway during toxin–channel interaction, the energetic role of external K+ was examined in the association and dissociation kinetics. A high-affinity Shaker K427E-VGKC variant was expressed in Xenopus oocytes, and its activity was monitored via two-electrode voltage clamp between ∼10 and ∼30°C. Nanomolar applications of CTX to open and closed channels, in the presence of high external Na+ or high K+ concentrations, were used to measure blockade kinetics at different voltages and temperatures. In high K+, both the dissociation and association rates showed higher activation enthalpies, by ∼15 kJ/mol and ∼25 kJ/mol, respectively, compared with high Na+ conditions. However, the association rates under high Na+ and K+ were equal at ∼20°C, indicating a compensatory K+-induced activation entropy. We propose transient CTX-wobbling intermediates in both directions of the reaction pathway. Such a wobbling intermediate could enhance the diversity of productive collisions during association, increasing the efficacy of the scorpion venom.
Figueroa, Juan David; Schejtman, Sergio D. Garcia; Tu, Ryan; Muñoz, Marcelo; Salas-Sepúlveda, Francisca; Poblete, Horacio; Langlois, Marc-André; Suuronen, Erik J.; Alarcon, Emilio I.
Ultrashort Peptides as Stabilizing Agents for Colloidal Nanogold Artículo de revista
En: 2025.
@article{Figueroa2025,
title = {Ultrashort Peptides as Stabilizing Agents for Colloidal Nanogold},
author = {Juan David Figueroa and Sergio D. Garcia Schejtman and Ryan Tu and Marcelo Muñoz and Francisca Salas-Sepúlveda and Horacio Poblete and Marc-André Langlois and Erik J. Suuronen and Emilio I. Alarcon},
doi = {10.1021/acsami.4c17794},
year = {2025},
date = {2025-03-25},
urldate = {2025-03-25},
abstract = {Ultrashort peptides hold immense potential as structural tools for enhancing the colloidal stability of nanomaterials, such as nanogold. However, such applications have been largely unexplored in part due to the inherent complexity in designing, synthesizing, and testing short peptides as colloidal nanoparticle stabilizers. In this work, we use a motif-function-guided process for peptide synthesis and high throughput screening to evaluate the colloidal stability of spherical nanogold solutions and pentapeptides. We have successfully built a library of peptides capable of stabilizing colloidal nanogold at peptide concentrations of ≤1.0 μM. This represents a 50–100-fold reduction in the concentration required for stability compared to other small molecules used as capping agents, which illustrates the potential of using short peptide sequences as colloidal nanogold stabilizers. Our findings could significantly impact the future development of high-affinity surface modifiers for the custom engineering of nanogold by providing a deeper understanding of the complex interactions between nanoparticles and peptides.
},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Ultrashort peptides hold immense potential as structural tools for enhancing the colloidal stability of nanomaterials, such as nanogold. However, such applications have been largely unexplored in part due to the inherent complexity in designing, synthesizing, and testing short peptides as colloidal nanoparticle stabilizers. In this work, we use a motif-function-guided process for peptide synthesis and high throughput screening to evaluate the colloidal stability of spherical nanogold solutions and pentapeptides. We have successfully built a library of peptides capable of stabilizing colloidal nanogold at peptide concentrations of ≤1.0 μM. This represents a 50–100-fold reduction in the concentration required for stability compared to other small molecules used as capping agents, which illustrates the potential of using short peptide sequences as colloidal nanogold stabilizers. Our findings could significantly impact the future development of high-affinity surface modifiers for the custom engineering of nanogold by providing a deeper understanding of the complex interactions between nanoparticles and peptides.
Galaz-Araya, Constanza; Zúñiga-Núñez, Daniel; Salas-Sepúlveda, Francisca; Herrera-Morande, Alejandra; Aspée, Alexis; Poblete, Horacio; Zamora, Ricardo A.
En: 2025.
@article{Galaz-Araya2025b,
title = {Theoretical evaluation of a bulky ortho-thioalkyl-azobenzene as an alternative to photocontrol structural cytotoxic effects of metal-free and disulfide oxidized hSOD1 in pathogenesis of ALS},
author = {Constanza Galaz-Araya and Daniel Zúñiga-Núñez and Francisca Salas-Sepúlveda and Alejandra Herrera-Morande and Alexis Aspée and Horacio Poblete and Ricardo A. Zamora },
doi = {10.1039/D4RA08972C},
year = {2025},
date = {2025-03-24},
urldate = {2025-03-24},
abstract = {This study presents a novel photopharmacological strategy to mitigate the cytotoxic effects of apo-hSOD1S–S, a misfolded protein implicated in neurodegenerative diseases. Using quantum chemical calculations and molecular dynamics simulations, we demonstrate that ortho-thio-substituted azobenzene photoswitches (ortho-TABPs) can be employed to precisely modulate the dynamics of the crucial electrostatic loop (EL) in apo-hSOD1S–S. We establish that larger ortho-S-alkyl substituents on the ortho-TABP enhance its redox stability, favouring the cis conformation through the modulation of the position of the n → π* transition. This stability is crucial for operation within the reducing cellular environment. Furthermore, we demonstrate the successful and consistent photomodulation of EL conformational dynamics in apo-hSOD1S–S through covalent tethering of an ortho-TABP. This control is achieved by leveraging the thermodynamically stable trans conformation of the photoswitch, which allosterically influences the EL and consequently, the geometry of the Zn-binding site, a critical determinant of apo-hSOD1S–S cytotoxicity. This work paves the way for developing targeted therapies for neurodegenerative diseases by demonstrating the precise and effective photomodulation of apo-hSOD1S–S via rationally designed ortho-TABPs.
},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
This study presents a novel photopharmacological strategy to mitigate the cytotoxic effects of apo-hSOD1S–S, a misfolded protein implicated in neurodegenerative diseases. Using quantum chemical calculations and molecular dynamics simulations, we demonstrate that ortho-thio-substituted azobenzene photoswitches (ortho-TABPs) can be employed to precisely modulate the dynamics of the crucial electrostatic loop (EL) in apo-hSOD1S–S. We establish that larger ortho-S-alkyl substituents on the ortho-TABP enhance its redox stability, favouring the cis conformation through the modulation of the position of the n → π* transition. This stability is crucial for operation within the reducing cellular environment. Furthermore, we demonstrate the successful and consistent photomodulation of EL conformational dynamics in apo-hSOD1S–S through covalent tethering of an ortho-TABP. This control is achieved by leveraging the thermodynamically stable trans conformation of the photoswitch, which allosterically influences the EL and consequently, the geometry of the Zn-binding site, a critical determinant of apo-hSOD1S–S cytotoxicity. This work paves the way for developing targeted therapies for neurodegenerative diseases by demonstrating the precise and effective photomodulation of apo-hSOD1S–S via rationally designed ortho-TABPs.
Galaz-Araya, Constanza; Galaz-Davison, Pablo; Cortés-Arriagada, Diego; Zamora, Ricardo A.; Poblete, Horacio
Molecular Dynamics Study on the Influence of the CLK Motif on the Structural Stability of Collagen-Like Peptides Adsorbed on Gold Nanosurfaces Artículo de revista
En: ACS Omega, vol. 10, no 10, pp. 10366–10374, 2025, ISSN: 2470-1343.
@article{Galaz-Araya2025,
title = {Molecular Dynamics Study on the Influence of the CLK Motif on the Structural Stability of Collagen-Like Peptides Adsorbed on Gold Nanosurfaces},
author = {Constanza Galaz-Araya and Pablo Galaz-Davison and Diego Cortés-Arriagada and Ricardo A. Zamora and Horacio Poblete},
doi = {10.1021/acsomega.4c10450},
issn = {2470-1343},
year = {2025},
date = {2025-03-18},
journal = {ACS Omega},
volume = {10},
number = {10},
pages = {10366--10374},
publisher = {American Chemical Society (ACS)},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
2024
Zuñiga-Bustos, Matias; Galaz-Araya, Constanza; Poblete, Horacio
Unveiling the Potential of RADA16-I Peptide-Coated Silver Nanoparticles for Biomedical Uses: A Computational Study Artículo de revista
En: Phys. Chem. Chem. Phys., 2024, ISSN: 1463-9084.
@article{Zuñiga-Bustos2024,
title = {Unveiling the Potential of RADA16-I Peptide-Coated Silver Nanoparticles for Biomedical Uses: A Computational Study},
author = {Matias Zuñiga-Bustos and Constanza Galaz-Araya and Horacio Poblete},
doi = {10.1039/d4cp03275f},
issn = {1463-9084},
year = {2024},
date = {2024-12-10},
urldate = {2024-00-00},
journal = {Phys. Chem. Chem. Phys.},
publisher = {Royal Society of Chemistry (RSC)},
abstract = {<jats:p>Nanomaterials, specifically silver nanoparticles (AgNPs), have demonstrated great potential in biomedical applications due to their unique properties, such as antimicrobial activity and conductivity. One promising strategy to improve their biocompatibility...</jats:p>},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
<jats:p>Nanomaterials, specifically silver nanoparticles (AgNPs), have demonstrated great potential in biomedical applications due to their unique properties, such as antimicrobial activity and conductivity. One promising strategy to improve their biocompatibility...</jats:p>
Ross, Alex; Guo, Xixi; Salazar, German A. Mercado; Schejtman, Sergio David Garcia; El-Hage, Jinane; Comtois-Bona, Maxime; Macadam, Aidan; Guzman-Soto, Irene; Takaya, Hiroki; Hu, Kevin; Liu, Bryan; Tu, Ryan; Siddiqi, Bilal; Anderson, Erica; Muñoz, Marcelo; Briones-Rebolledo, Patricio; Ning, Tianqin; Griffith, May; Rotsein, Benjamin; Poblete, Horacio; Li, Jianyu; Ruel, Marc; Suuronen, Erik J.; Alarcon, Emilio I.
Multipurpose On-the-Spot Peptide-Based Hydrogels for Skin, Cornea, and Heart Repair Artículo de revista
En: Advanced Functional Materials, vol. 34, no 37, pp. 2402564, 2024, (_eprint: https://onlinelibrary.wiley.com/doi/pdf/10.1002/adfm.202402564).
@article{ross_multipurpose_2024,
title = {Multipurpose On-the-Spot Peptide-Based Hydrogels for Skin, Cornea, and Heart Repair},
author = {Alex Ross and Xixi Guo and German A. Mercado Salazar and Sergio David Garcia Schejtman and Jinane El-Hage and Maxime Comtois-Bona and Aidan Macadam and Irene Guzman-Soto and Hiroki Takaya and Kevin Hu and Bryan Liu and Ryan Tu and Bilal Siddiqi and Erica Anderson and Marcelo Muñoz and Patricio Briones-Rebolledo and Tianqin Ning and May Griffith and Benjamin Rotsein and Horacio Poblete and Jianyu Li and Marc Ruel and Erik J. Suuronen and Emilio I. Alarcon},
url = {https://onlinelibrary.wiley.com/doi/abs/10.1002/adfm.202402564},
doi = {https://doi.org/10.1002/adfm.202402564},
year = {2024},
date = {2024-01-01},
journal = {Advanced Functional Materials},
volume = {34},
number = {37},
pages = {2402564},
abstract = {Abstract Bioinspired synthetic materials can be designed as reliable, cost-effective, and fully controlled alternatives to natural biomaterials for treating damaged tissues and organs. However, several hurdles need to be overcome for clinical translation, particularly for biomaterials gelled in situ. These include the potential toxicity of chemical crosslinkers used in the materials' assembly or breakdown products they generate and the challenges of fine-tuning the mechanical properties of the materials. Here, a minimalistic, adhesive soft material is developed by screening hundreds of potential formulations of self-assembling, custom-designed collagen-like peptide sequences for the in situ formation of tissue-bonding 3D hydrogels. Nine promising formulations for tissue repair are identified using a low-volume and rapid combinatory screening approach. It is shown that simply varying the ratio of the two key components promotes adhesion and fine-tunes the material's mechanical properties. The materials' skin and heart repair capabilities are assessed in vitro and clinically relevant animal models. The materials are also tested for corneal applications using ex vivo pig cornea models complemented by in vitro cell compatibility assays.},
note = {_eprint: https://onlinelibrary.wiley.com/doi/pdf/10.1002/adfm.202402564},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
Abstract Bioinspired synthetic materials can be designed as reliable, cost-effective, and fully controlled alternatives to natural biomaterials for treating damaged tissues and organs. However, several hurdles need to be overcome for clinical translation, particularly for biomaterials gelled in situ. These include the potential toxicity of chemical crosslinkers used in the materials' assembly or breakdown products they generate and the challenges of fine-tuning the mechanical properties of the materials. Here, a minimalistic, adhesive soft material is developed by screening hundreds of potential formulations of self-assembling, custom-designed collagen-like peptide sequences for the in situ formation of tissue-bonding 3D hydrogels. Nine promising formulations for tissue repair are identified using a low-volume and rapid combinatory screening approach. It is shown that simply varying the ratio of the two key components promotes adhesion and fine-tunes the material's mechanical properties. The materials' skin and heart repair capabilities are assessed in vitro and clinically relevant animal models. The materials are also tested for corneal applications using ex vivo pig cornea models complemented by in vitro cell compatibility assays.
2023
Zúñiga-Núñez, Daniel; Mura, Francisco; Mariño-Ocampo, Nory; Briones-Rebolledo, Patricio; Poblete, Horacio; Mallet, Jean-Maurice; Fuentealba, Denis; Aspée, Alexis
Time-resolved fluorescence and anisotropy-sensitive 1,2-dimyristoyl-sn-glycero-3-(7-aminocoumarin) phosphoetanolamide probe for studying membrane lipid domains Artículo de revista
En: Dyes and Pigments, vol. 217, pp. 111368, 2023, ISSN: 0143-7208.
@article{zuniga-nunez_time-resolved_2023,
title = {Time-resolved fluorescence and anisotropy-sensitive 1,2-dimyristoyl-sn-glycero-3-(7-aminocoumarin) phosphoetanolamide probe for studying membrane lipid domains},
author = {Daniel Zúñiga-Núñez and Francisco Mura and Nory Mariño-Ocampo and Patricio Briones-Rebolledo and Horacio Poblete and Jean-Maurice Mallet and Denis Fuentealba and Alexis Aspée},
url = {https://www.sciencedirect.com/science/article/pii/S0143720823002942},
doi = {https://doi.org/10.1016/j.dyepig.2023.111368},
issn = {0143-7208},
year = {2023},
date = {2023-01-01},
journal = {Dyes and Pigments},
volume = {217},
pages = {111368},
abstract = {A fluorescent probe C-DMPE was synthesised to monitor interfacial membrane properties by conjugating coumarin-343 and 1,2-dimyristoyl-sn-glycero-3-phosphorylethanolamine (DMPE), anchoring the 7-aminocoumarin moiety close to the phospholipid polar head at the membrane interface. Large unilamellar vesicles (LUV) of 1,2-dipalmitoyl-sn-glycero-3-phosphatidylcholine (DPPC), of 1,2-dioleyl-sn-glycero-3-phosphatidylcholine (DOPC) and cholesterol were employed as a model of lipid bilayer. Time-resolved fluorescence developed an emissive Internal Charge Transfer excited state with a long fluorescence lifetime (τ1), a Locally Excited state with an intermediate fluorescence lifetime (τ2), and a short lifetime (τ3) associated with an intermolecular quenching by interaction with a phosphate group of neighbour phospholipids, as is clearly shown by molecular dynamics simulations. Shorter values of fluorescence lifetimes τ1 and τ3 were observed in DOPC with respect to DPPC, responding to a more fluid membrane with more significant water accessibility in DOPC than DPPC. However, in DPPC:DOPC vesicles, these fluorescence lifetimes are even shorter, allowing to be attributed to favourable sensing of boundary limit lipid domains. In similitude, time-resolved anisotropy showed shorter rotational correlation times φ1, in DPPC: DOPC vesicles than in DOPC associated with a faster internal rotational movement of the 7-aminocoumarin group in domains than in fluid a DOPC membrane. In addition, shorter rotational correlation times, φ2, were also observed in DPPC:DOPC vesicles compared to DPPC, suggesting a faster lateral diffusion of the probe in the presence of domains.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
A fluorescent probe C-DMPE was synthesised to monitor interfacial membrane properties by conjugating coumarin-343 and 1,2-dimyristoyl-sn-glycero-3-phosphorylethanolamine (DMPE), anchoring the 7-aminocoumarin moiety close to the phospholipid polar head at the membrane interface. Large unilamellar vesicles (LUV) of 1,2-dipalmitoyl-sn-glycero-3-phosphatidylcholine (DPPC), of 1,2-dioleyl-sn-glycero-3-phosphatidylcholine (DOPC) and cholesterol were employed as a model of lipid bilayer. Time-resolved fluorescence developed an emissive Internal Charge Transfer excited state with a long fluorescence lifetime (τ1), a Locally Excited state with an intermediate fluorescence lifetime (τ2), and a short lifetime (τ3) associated with an intermolecular quenching by interaction with a phosphate group of neighbour phospholipids, as is clearly shown by molecular dynamics simulations. Shorter values of fluorescence lifetimes τ1 and τ3 were observed in DOPC with respect to DPPC, responding to a more fluid membrane with more significant water accessibility in DOPC than DPPC. However, in DPPC:DOPC vesicles, these fluorescence lifetimes are even shorter, allowing to be attributed to favourable sensing of boundary limit lipid domains. In similitude, time-resolved anisotropy showed shorter rotational correlation times φ1, in DPPC: DOPC vesicles than in DOPC associated with a faster internal rotational movement of the 7-aminocoumarin group in domains than in fluid a DOPC membrane. In addition, shorter rotational correlation times, φ2, were also observed in DPPC:DOPC vesicles compared to DPPC, suggesting a faster lateral diffusion of the probe in the presence of domains.
2022
Rosales-Rojas, Roberto; Zuñiga-Bustos, Matías; Salas-Sepúlveda, Francisca; Galaz-Araya, Constanza; Zamora, Ricardo A.; Poblete, Horacio
Self-Organization Dynamics of Collagen-like Peptides Crosslinking Is Driven by Rose-Bengal-Mediated Electrostatic Bridges Artículo de revista
En: Pharmaceutics, vol. 14, no 6, pp. 1148, 2022, ISSN: 1999-4923.
@article{rosales-rojas_self-organization_2022,
title = {Self-Organization Dynamics of Collagen-like Peptides Crosslinking Is Driven by Rose-Bengal-Mediated Electrostatic Bridges},
author = {Roberto Rosales-Rojas and Matías Zuñiga-Bustos and Francisca Salas-Sepúlveda and Constanza Galaz-Araya and Ricardo A. Zamora and Horacio Poblete},
url = {https://www.mdpi.com/1999-4923/14/6/1148},
doi = {10.3390/pharmaceutics14061148},
issn = {1999-4923},
year = {2022},
date = {2022-05-01},
urldate = {2025-01-02},
journal = {Pharmaceutics},
volume = {14},
number = {6},
pages = {1148},
abstract = {The present work focuses on the computational study of the structural micro-organization of hydrogels based on collagen-like peptides (CLPs) in complex with Rose Bengal (RB). In previous studies, these hydrogels computationally and experimentally demonstrated that when RB was activated by green light, it could generate forms of stable crosslinked structures capable of regenerating biological tissues such as the skin and cornea. Here, we focus on the structural and atomic interactions of two collagen-like peptides (collagen-like peptide I (CLPI), and collagen-like peptide II, (CLPII)) in the presence and absence of RB, highlighting the acquired three-dimensional organization and going deep into the stabilization effect caused by the dye. Our results suggest that the dye could generate a ternary ground-state complex between collagen-like peptide fibers, specifically with positively charged amino acids (Lys in CLPI and Arg in CLPII), thus stabilizing ordered three-dimensional structures. The discoveries generated in this study provide the structural and atomic bases for the subsequent rational development of new synthetic peptides with improved characteristics for applications in the regeneration of biological tissues during photochemical tissue bonding therapies.},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
The present work focuses on the computational study of the structural micro-organization of hydrogels based on collagen-like peptides (CLPs) in complex with Rose Bengal (RB). In previous studies, these hydrogels computationally and experimentally demonstrated that when RB was activated by green light, it could generate forms of stable crosslinked structures capable of regenerating biological tissues such as the skin and cornea. Here, we focus on the structural and atomic interactions of two collagen-like peptides (collagen-like peptide I (CLPI), and collagen-like peptide II, (CLPII)) in the presence and absence of RB, highlighting the acquired three-dimensional organization and going deep into the stabilization effect caused by the dye. Our results suggest that the dye could generate a ternary ground-state complex between collagen-like peptide fibers, specifically with positively charged amino acids (Lys in CLPI and Arg in CLPII), thus stabilizing ordered three-dimensional structures. The discoveries generated in this study provide the structural and atomic bases for the subsequent rational development of new synthetic peptides with improved characteristics for applications in the regeneration of biological tissues during photochemical tissue bonding therapies.
2019
Goel, Keshav; Zuñiga-Bustos, Matias; Lazurko, Caitlin; Jacques, Erik; Galaz-Araya, Constanza; Valenzuela-Henriquez, Francisco; Pacioni, Natalia L.; Couture, Jean-François; Poblete, Horacio; Alarcon, Emilio I.
Nanoparticle Concentration vs Surface Area in the Interaction of Thiol-Containing Molecules: Toward a Rational Nanoarchitectural Design of Hybrid Materials Artículo de revista
En: ACS Applied Materials & Interfaces, vol. 11, no 19, pp. 17697–17705, 2019, ISSN: 1944-8244, 1944-8252.
@article{goel_nanoparticle_2019,
title = {Nanoparticle Concentration vs Surface Area in the Interaction of Thiol-Containing Molecules: Toward a Rational Nanoarchitectural Design of Hybrid Materials},
author = {Keshav Goel and Matias Zuñiga-Bustos and Caitlin Lazurko and Erik Jacques and Constanza Galaz-Araya and Francisco Valenzuela-Henriquez and Natalia L. Pacioni and Jean-François Couture and Horacio Poblete and Emilio I. Alarcon},
url = {https://pubs.acs.org/doi/10.1021/acsami.9b03942},
doi = {10.1021/acsami.9b03942},
issn = {1944-8244, 1944-8252},
year = {2019},
date = {2019-05-01},
urldate = {2025-01-02},
journal = {ACS Applied Materials & Interfaces},
volume = {11},
number = {19},
pages = {17697–17705},
keywords = {},
pubstate = {published},
tppubtype = {article}
}
