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The properties of nanoparticle superstructures depend on many factors, including the structural metrics of the nanoparticle superstructure (particle diameter, interparticle distances, etc.). Here, we introduce a family of gold-binding peptide conjugate molecules that can direct nanoparticle assembly, and we describe how these molecules can be systematically modified to adjust the structural metrics of linear double-helical nanoparticle superstructures. Twelve new peptide conjugates are prepared via linking a gold-binding peptide, AYSSGAPPMPPF (PEP(Au)), to a hydrophobic aliphatic tail. The peptide conjugates have 1, 2, or 3 PEP(Au) headgroups and a C12, C14, C16, or C18 aliphatic tail. The soft assembly of these peptide conjugates was studied using transmission electron microscopy (TEM), atomic force microscopy (AFM), and infrared (IR) spectroscopy. Several peptide conjugates assemble into 1-D twisted fibers having measurable structural parameters such as fiber width, thickness, and pitch that can be systematically varied by adjusting the aliphatic tail length and number of peptide headgroups. The linear soft assemblies serve as structural scaffolds for arranging gold nanoparticles into double-helical superstructures, which are examined via TEM. The pitch and interparticle distances of the gold nanoparticle double helices correspond to the underlying metrics of the peptide conjugate soft assemblies, illustrating that designed peptide conjugate molecules can be used to not only direct the assembly of gold nanoparticles but also control the metrics of the assembled structure.
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http://dx.doi.org/10.1021/acs.langmuir.5b02208 | DOI Listing |
Sci Adv
September 2025
School of Electrical and Electronic Engineering, Yonsei University, 50-1 Yonsei-ro, Seodaemun-gu, Seoul 03722, Republic of Korea.
Brain-computer interfaces (BCIs) enable direct communication between the brain and computers. However, their long-term functionality remains limited due to signal degradation caused by acute insertion trauma, chronic foreign body reaction (FBR), and biofouling at the device-tissue interface. To address these challenges, we introduce a multifunctional surface modification strategy called targeting-specific interaction and blocking nonspecific adhesion (TAB) coating for flexible fiber, achieving a synergistic integration of mechanical compliance and biochemical stability.
View Article and Find Full Text PDFBioconjug Chem
September 2025
Pôle Chimie Balard, IBMM - UMR 5247, 1919, Route de Mende, 34293 Montpellier cedex 5, France.
Phosphole-based fluorophores are attractive dyes for bioimaging due to their relatively compact molecular structures, strong fluorescence up to the near-infrared region with large Stokes shifts, and remarkable resistance to photobleaching. Therefore, the development of efficient and chemoselective coupling methods for functionalizing phospholes is of significant interest for biomolecular labeling. Herein, we describe the synthesis of novel P-aminophospholes and their use for direct conjugation to cysteinyl peptides under mild conditions.
View Article and Find Full Text PDFMater Today Bio
October 2025
Yunnan Key Laboratory of Breast Cancer Precision Medicine, Institute of Biomedical Engineering, Kunming Medical University, Kunming, 650500, Yunnan, China.
Achieving precise intratumoral accumulation and coordinated activation remains a major challenge in nanomedicine. Photothermal therapy (PTT) provides spatiotemporal control, yet its efficacy is hindered by heterogeneous distribution of PTT agents and limited synergy with other modalities. Here, we develop a dual-activation nanoplatform (IrO-P) that integrates exogenous photothermal stimulation with endogenous tumor microenvironment (TME)-responsive catalysis for synergistic chemodynamic therapy (CDT) and ferroptosis induction.
View Article and Find Full Text PDFCell Physiol Biochem
September 2025
Charité - Universitätsmedizin Berlin, corporate member of Freie Universität Berlin and Humboldt-Universität zu Berlin, Institute of Biochemistry, 10117 Berlin, Germany.
Background/aims: The ubiquitin-like protein ISG15 and its covalent conjugation to substrates (ISGylation) represent a critical interferon (IFN)-induced antiviral mechanism. USP18 is an ISG15-specific isopeptidase and a key negative regulator of type I IFN signaling. While inactivation of USP18's catalytic activity enhances ISGylation and promotes viral resistance, its role in modulating inflammation and cardiac function during CVB3-induced myocarditis remains unclear.
View Article and Find Full Text PDFInt J Biol Macromol
September 2025
Department of Chemical & Biochemical Engineering, Dongguk University, Seoul, 04620, Republic of Korea. Electronic address:
Modified hyaluronic acid (HA) biomaterials have received considerable attention in recent years, especially in developing innovative therapeutic strategies for targeted disease interventions. HA serves to shield therapeutics from the physiological environment, while enabling safe delivery and promoting uptake into specific cells. As a hydrophilic chain polymer, HA is readily chemically modified into functional biomaterials for drug delivery and cancer immunotherapy.
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