@article{202602.1170,

title = {QCM Genosensor for Detection of Golden Mosaic-Resistant Transgenic Common Beans in Non-Amplified Samples},

author = {Isabella C. S. Nascimento and Andressa M. Souza and Andrea P. Parente and Edna M. M. Oliveira and Andrea Valdman and Rossana O. M. Folly and Andrea M. Salgado},

url = {https://doi.org/10.20944/preprints202602.1170.v1},

doi = {10.20944/preprints202602.1170.v1},

year  = {2026},

date = {2026-02-14},

urldate = {2026-02-14},

journal = {Preprints},

publisher = {Preprints},

abstract = {A quartz crystal microbalance-based biosensor for the specific detection of the first transgenic

common bean (Phaseolus vulgaris L.) cultivar (BRS FC401 RMD) with resistance to bean golden mosaic

virus (BGMV) was developed. The immobilization chemistry relies on the strong bond between the

thiolated probe and the gold electrode surface. The probe sequence is internal to a region of the

BGMV rep gene that was introduced into the common bean genome. The sensor's analytical

performance was determined using synthetic oligonucleotides. Real samples of transgenic and wild-

type bean seeds were also tested. Sample pretreatment consisted only of enzymatic fragmentation,

followed by a thermal denaturation step combined with blocking oligonucleotides. Different

biosensor regeneration approaches were studied. Immobilization showed good reproducibility

(CV% of 5.8%). The biosensor proved specific for both synthetic oligonucleotides and non-amplified

genomic DNA. A linear detection range of 0–1.4 ng/µL was observed, with a detection limit of 0.18

ng/µL. Three sequential detections were performed without loss of surface activity. The results

demonstrate the biosensor's potential for direct, real-time, label-free detection of DNA samples for

field screening of transgenic common bean cultivars.},

keywords = {bean golden mosaic virus, Biosensor, common bean, genetically modified organism, Immobilization, openQCM, openQCM Software, Quartz Crystal Microbalance (QCM), regeneration},

pubstate = {published},

tppubtype = {article}

}

@article{doi:10.1021/acs.biomac.5c00010,

title = {Controlling Protein Immobilization over Poly(3-hydroxybutyrate) Microparticles Using Substrate Binding Domain from PHA Depolymerase},

author = {Isabela P. Dias and Regiane Stafim Cunha and Ryu Masaki and Maritza A. Todo Bom and Edneia A. S. Ramos and Giovanna J. V. P. Santos and Giovanna Furman and Julia T. Lucena and Isabella G. Jiacomini and Sze M. Lo and Zelinda Schemczssen-Graeff and Breno C. B. Beirão and Silvio M. Zanata and Luiz M. de L. Faria and Edileusa M. Gerhardt and Emanuel Maltempi Souza and Marcelo Müller-Santos and Guilherme F. Picheth},

url = {https://doi.org/10.1021/acs.biomac.5c00010},

doi = {10.1021/acs.biomac.5c00010},

year  = {2025},

date = {2025-03-09},

urldate = {2025-03-09},

journal = {Biomacromolecules},

abstract = {Biointerface decoration with ligands is a crucial requirement to modulate biodistribution, increase half-life, and provide navigation control for targeted micro- or nanostructured systems. To better control the process of ligand functionalization over three-dimensional (3D) polyester surfaces, we report the characterization of hybrid proteins developed to enhance the anchoring efficiency over polymeric surfaces and preserve optimal spatial orientation: sfGFP, mRFP1, and the RBD proteins were attached to a polyester substrate binding domain (SBD) formed by the C-terminus region of PHA depolymerase. The binding ability was evaluated over poly(3-hydroxybutyrate) (PHB) microparticles (MP) and two-dimensional (2D) surfaces. The PHB interfaces revealed a high affinity toward the proteins linked with SBD, displaying higher protein contents compared to untagged proteins. The MP decorated with RBD-SBD exhibited limited MRC5 internalization and cytotoxicity without a significant impact caused by the RBD protein, suggesting that the system might be adapted for targeted drug delivery and vaccine applications.},

note = {PMID: 40059311},

keywords = {Immobilization, Ligands, Microparticles, openQCM Shield, Peptides and proteins, QCM, Quartz Crystal Microbalance, Toxicity},

pubstate = {published},

tppubtype = {article}

}