@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}

}

@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}

}

@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}

}

@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}

}