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Instant and strong adhesion to underwater adherends is a big challenge due to the continuous interference of water. Mussel foot protein-bioinspired catechol-based adhesives have garnered great interest in addressing this issue. Herein, a novel self-made catecholic compound with a long aliphatic chain was utilized to prepare thin (∼0.07 mm) and optically transparent (>80%) wet/underwater adhesive tapes by UV-initiated polymerization. Its adhesion activity was water-triggered, fast (<1 min), and strong (adhesion strength to porcine skin: ∼1.99 MPa; interfacial toughness: ∼610 J/m, burst pressure: ∼1950 mmHg). The effect of the catechol/phenol group and positively charged moiety on the wet/underwater adhesion to abiotic/biotic substrates was investigated. On the wet/underwater adherends, the tape with catechol groups presented much higher interfacial toughness, adhesion strength, and burst pressure than the analogous tape with phenol groups. The tape with both the catechol group and cationic polyelectrolyte chitosan had a more impressive improvement in its adhesion to wet/underwater biological tissues than to abiotic substrates. Therefore, catechol and a positive moiety in the tape would synergistically enhance its wet/underwater adhesion to various substrates, especially to biological tissues. The instant, strong, and noncytotoxic tape may provide applications in underwater adhesion for sealing and wound closure.
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http://dx.doi.org/10.1021/acsami.4c09709 | DOI Listing |
Colloids Surf B Biointerfaces
August 2025
Department of Orthopedics, Affiliated Hospital of Jiangxi University of Chinese Medicine, Nanchang, Jiangxi 330006, China. Electronic address:
Infected wounds remain a major clinical challenge due to bacterial invasion, which disrupts the natural healing cascade through excessive reactive oxygen species (ROS) generation, severe vascular damage, and persistent inflammation. Inspired by the catechol-rich adhesive domains of mussel foot proteins, we developed an extracellular matrix (ECM)-mimetic polyethylene glycol (PEG) hydrogel incorporating polydopamine (PDA)-functionalized zinc oxide nanoparticles (ZnONPs) for infected wound therapy. The amino acid-functionalized PEG hydrogel reproduces ECM-like properties to facilitate cell migration and efficient exudate management; however, its lack of intrinsic antimicrobial activity limits therapeutic efficacy.
View Article and Find Full Text PDFIn this letter, the pull-off forces of adsorbed films of four Bap1-inspired peptides in various solvents were investigated on negatively charged mica substrates using the surface forces apparatus (SFA), complemented with dynamic light scattering (DLS) for characterizing the aggregation behavior of peptides in solution. Bap1-inspired peptides consisted of the 57 amino acid wild-type sequence (WT); a scrambled version of the WT used to investigate the impact of the primary amino acid sequence in pull-off forces (Scr); a ten amino acid sequence rich in hydrophobic content (CP) of the WT sequence, and an eight amino acid sequence (Sh1) that corresponds to the pseudo-repeating sequence in the 57 AA. SFA results showed remarkable pull-off forces for CP, particularly in the presence of salts: measured pull-off forces were 26.
View Article and Find Full Text PDFAntioxidants (Basel)
August 2025
Department of Marine Pharmacology, College of Food Science and Technology, Shanghai Ocean University, Shanghai 201306, China.
Chronic inflammation is closely associated with various diseases, underscoring the need for natural, biocompatible anti-inflammatory candidates. For this purpose, mussel foot protein could be an excellent candidate due to its diverse biological activities. Hence, this study systematically evaluates the anti-inflammatory effects of a highly soluble mussel foot protein (HMFP) and HMFP-PEG using LPS-stimulated RAW264.
View Article and Find Full Text PDFInt J Biol Macromol
September 2025
Department of Biochemistry and Biotechnology, Council of Scientific and Industrial Research (CSIR) - Central Leather Research Institute, Chennai, Tamil Nadu 600020, India; Academy of Scientific and Innovative Research (AcSIR), Ghaziabad 201002, India. Electronic address:
Mussel foot protein-5 (mfp-5) is a key biological macromolecule responsible for the remarkable ability of mussels to adhere to wet and diverse surfaces. While the function of L-3,4-dihydroxyphenylalanine (Dopa) in underwater adhesion is well-characterised, the structural and functional role of hydroxyproline (Hyp) in mfp-5 remains underexplored, largely due to challenges in achieving site-specific dual post-translational modifications (PTMs). In this study, we employed residue-specific genetic code expansion strategies to incorporate either Dopa or Hyp into mfp-5 and systematically analyzed their effects on liquid-liquid phase separation (LLPS), redox stability, and interfacial interactions.
View Article and Find Full Text PDFNano Lett
August 2025
SKKU Advanced Institute of Nanotechnology (SAINT), Sungkyunkwan University (SKKU), 2066 Seobu-ro, Jangan-gu, Suwon, Gyeonggi-do 16419, Republic of Korea.
The advancement of biomaterials through innovative surface functionalization techniques is essential for enhancing the performance and functionality. Recombinant adhesive proteins (RAPs), engineered from mussel foot proteins and antimicrobial peptides, present unique opportunities for surface functionalization of biomaterials. Here, we reveal a previously unexplored property of RAPs: fractal-like structural growth that promotes efficient surface coverage and functionalization.
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