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Macromol
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Advanced Functional Biomacromolecules in Biosensing
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Advanced Functional Biomacromolecules in Biosensing

A Special Issue of Macromol (ISSN 2673-6209).

Deadline for manuscript submissions: 30 November 2026 | Viewed by 2079

Editor

Dr. Felismina Teixeira Coelho Moreira

E-Mail Website
Guest Editor
CIETI—LabRISE, ISEP, Polytechnic of Porto, Rua António Bernardino de Almeida, 431, 4249-015 Porto, Portugal
Interests: biosensors; biomimetic materials; electrochemistry and nanomaterials
Special Issues, Collections and Topics in MDPI journals

Special Issue Information

Dear Colleagues,

Biomacromolecules, such as nucleic acids, proteins, carbohydrates, and lipids, play essential roles in biological systems due to their intrinsic biocompatibility, structural diversity, and highly specific molecular recognition capabilities. These properties make them particularly attractive for developing advanced biosensing platforms that involve immobilizing or engineering advanced functional biomacromolecules at interfaces to precisely regulate molecular interactions, enabling increased selectivity, sensitivity, and stability.

This Special Issue highlights recent advances in the design, functionalization, and integration of advanced biomacromolecules for biosensing applications. Topics of interest include innovative immobilization strategies, biointerface engineering, signal amplification mechanisms, antifouling approaches, and emerging diagnostic technologies.

By bringing together interdisciplinary contributions, this Special Issue provides a comprehensive overview of current challenges and future perspectives in developing next-generation biomacromolecule-based biosensors.

You may choose our Joint Special Issue in Polymers.

Dr. Felismina Teixeira Coelho Moreira
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 250 words) can be sent to the Editorial Office for assessment.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-anonymized peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Macromol is an international peer-reviewed open access quarterly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 1200 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • biomacromolecules
  • biosensors
  • proteins
  • carbohydrates
  • nucleic acids

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Published Papers (3 papers)

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Research

19 pages, 13691 KB  
Article
Pectin-Based Flexible and Wearable Bioelectrodes for EMG Signal Recording
by Pasha W. Sayyad, Meera Alex, Amani Al-Othman, Hasan Al-Nashash and Mohammad H. Al-Sayah
Macromol 2026, 6(3), 64; https://doi.org/10.3390/macromol6030064 - 18 Aug 2026
Viewed by 209
Abstract
Pectin, a natural biopolymer, is a cost-effective, biocompatible, non-toxic, abundant, and flexible material, making it suitable for recording high-quality bioelectric signals from the dynamic surface of the human body. In this work, pectin-based flexible bioelectrodes were developed for the non-invasive monitoring of biopotentials. [...] Read more.
Pectin, a natural biopolymer, is a cost-effective, biocompatible, non-toxic, abundant, and flexible material, making it suitable for recording high-quality bioelectric signals from the dynamic surface of the human body. In this work, pectin-based flexible bioelectrodes were developed for the non-invasive monitoring of biopotentials. The bioelectrodes are composed of pectin, polyaniline emeraldine salt (PANI-ES), glycerol, and polydimethylsiloxane (PDMS) and therefore abbreviated as PPGP. The PPGP electrodes demonstrated a bulk electrical conductivity of (7.54 ± 0.81) × 10−3 S/cm, a very low impedance of 34 Ω, and a high charge storage capacity of 4.63 ± 2.70 mC/cm2. The surface morphology of the PPGP electrode plays a crucial role in enhancing biopotential signal detection by improving adhesion to skin contours. PPGP electrodes have been successfully used for high-fidelity electromyographic (EMG) bioelectric signal measurements. The developed PPGP bioelectrodes have the potential to advance next-generation human–machine interface (HMI) technologies and wearable healthcare systems, including prosthetic control, rehabilitation monitoring, and assistive communication devices. Full article
(This article belongs to the Special Issue Advanced Functional Biomacromolecules in Biosensing)
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14 pages, 1916 KB  
Article
Gold Nanoparticle Glycointerfaces Functionalized with Alternating Glycopolymers Bearing Periodically Arranged Pendant Carbohydrate Residues
by Jin Motoyanagi, Junya Koga and Masahiko Minoda
Macromol 2026, 6(2), 43; https://doi.org/10.3390/macromol6020043 - 11 Jun 2026
Viewed by 653
Abstract
Alternating glycopolymers bearing periodically arranged pendant carbohydrate residues were synthesized by reversible addition–fragmentation chain transfer (RAFT) copolymerization of maltose-containing vinyl ether (MalVE) and ethyl maleimide (EtMI). The resulting trithiocarbonate-terminated polymers were subsequently converted into thiol-terminated glycopolymers through post-polymerization end-group transformation. These structurally well-defined [...] Read more.
Alternating glycopolymers bearing periodically arranged pendant carbohydrate residues were synthesized by reversible addition–fragmentation chain transfer (RAFT) copolymerization of maltose-containing vinyl ether (MalVE) and ethyl maleimide (EtMI). The resulting trithiocarbonate-terminated polymers were subsequently converted into thiol-terminated glycopolymers through post-polymerization end-group transformation. These structurally well-defined alternating glycopolymers were immobilized onto gold nanoparticles (AuNPs) via Au–S interactions to construct glycopolymer-functionalized glycointerfaces. Surface functionalization of the AuNPs was confirmed by an increase in hydrodynamic diameter from approximately 42 to 59 nm after polymer immobilization. The resulting glycopolymer-functionalized AuNPs exhibited concentration-dependent lectin-mediated aggregation behavior in the presence of concanavalin A, accompanied by characteristic red shifts and broadening of the localized surface plasmon resonance (LSPR) band arising from multivalent carbohydrate–lectin interactions at the nanoparticle interface. Although the apparent association constants obtained for free alternating glycopolymers using fluorescently labeled lectin cannot be directly compared with those obtained from LSPR-based aggregation assays of AuNP-immobilized glycopolymers, the values increased from the order of 105 L mol−1 in solution to the order of 107 L mol−1 at the nanoparticle interface. This trend suggests that immobilization onto AuNPs enhances multivalent carbohydrate–lectin interactions through multivalent presentation of the glycopolymer chains at the nanoparticle interface. As a control experiment, peanut agglutinin (PNA), which does not recognize maltose residues, was added to the glycopolymer-functionalized AuNPs. No significant LSPR shift or spectral broadening was observed, indicating that nanoparticle aggregation was not induced by nonspecific lectin addition but arose from specific interactions between maltose residues and Con A. Quantitative analysis suggested that polymer chain length may influence the aggregation behavior. These results demonstrate that alternating glycopolymers provide a useful platform for constructing sequence-regulated glycointerfaces and for investigating multivalent biomolecular interactions at nanoparticle surfaces. Full article
(This article belongs to the Special Issue Advanced Functional Biomacromolecules in Biosensing)
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17 pages, 3607 KB  
Article
Conformational Dynamics and Catalytic Behavior of Cysteine Proteases Immobilized on Alginate-Based Graft Copolymers: A Structure–Property Study
by Maria S. Lavlinskaya, Andrey V. Sorokin, Anastasia N. Dubovitskaya, Sofia S. Stepanova, Maxim S. Kondratyev, Marina G. Holyavka, Yuriy F. Zuev and Valeriy G. Artyukhov
Macromol 2026, 6(2), 40; https://doi.org/10.3390/macromol6020040 - 8 Jun 2026
Viewed by 645
Abstract
Cysteine proteases (bromelain, ficin, and papain) are widely used in biotechnology and medicine, but their application is limited by rapid autolysis and oxidative inactivation. This study aimed to develop effective supports for these enzymes based on graft copolymers of sodium alginate and poly( [...] Read more.
Cysteine proteases (bromelain, ficin, and papain) are widely used in biotechnology and medicine, but their application is limited by rapid autolysis and oxidative inactivation. This study aimed to develop effective supports for these enzymes based on graft copolymers of sodium alginate and poly(N-vinylpyrrolidone) (SA-g-PVP) and to elucidate the structure–property relationships governing immobilization efficiency, catalytic activity, and storage stability. Copolymers were synthesized via radical solution polymerization under optimized conditions. Enzymes were immobilized by physical adsorption, and the resulting complexes were characterized by Fourier-transform infrared (FTIR) spectroscopy, protein content assays, proteolytic and amidase activity measurements, and molecular docking. The graft copolymer with a smaller particle size in solution provided a larger accessible surface area, leading to higher bromelain and papain loading. Ficin showed the opposite trend due to its unique surface amino acid composition. Immobilization dramatically increased storage stability: half-life values for bromelain, ficin, and papain reached up to 20, 14, and 14 days, respectively, compared to 1–3 days for the free enzymes. Molecular docking revealed that the dense polymer shell stabilizes the enzyme tertiary structure by forming multiple contacts with internal cavities and tunnels, thereby preventing autolysis and conformational unfolding. Collectively, these findings demonstrate that SA-g-PVP copolymers are promising, non-toxic supports for cysteine proteases, with ficin showing up to 100% activity recovery, making them suitable for food, cosmetic, and biomedical applications. Full article
(This article belongs to the Special Issue Advanced Functional Biomacromolecules in Biosensing)
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