Microfluidic confinement enables monitoring of oligomeric forms of 1-40 β-amyloid peptide in kinetic study by AFM.

Greco P, Lazar AN, Lugli F, Albonetti C, Bystrenova E, Bianchi M, Fadiga L, Zerbetto F, Biscarini F

Open source

DOI
10.1016/j.jcis.2026.141599
Published
2026 Sep 14
Container
Journal of colloid and interface science
Publisher
Not recorded
Open access
unknown

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BibTeX

@article{allodium:10.1016/j.jcis.2026.141599,
  title = {Microfluidic confinement enables monitoring of oligomeric forms of 1-40 β-amyloid peptide in kinetic study by AFM.},
  author = {Greco P and Lazar AN and Lugli F and Albonetti C and Bystrenova E and Bianchi M and Fadiga L and Zerbetto F and Biscarini F},
  year = {2026},
  journal = {Journal of colloid and interface science},
  doi = {10.1016/j.jcis.2026.141599},
  url = {https://doi.org/10.1016/j.jcis.2026.141599}
}

RIS

TY  - JOUR
TI  - Microfluidic confinement enables monitoring of oligomeric forms of 1-40 β-amyloid peptide in kinetic study by AFM.
AU  - Greco P
AU  - Lazar AN
AU  - Lugli F
AU  - Albonetti C
AU  - Bystrenova E
AU  - Bianchi M
AU  - Fadiga L
AU  - Zerbetto F
AU  - Biscarini F
PY  - 2026
JO  - Journal of colloid and interface science
DO  - 10.1016/j.jcis.2026.141599
UR  - https://doi.org/10.1016/j.jcis.2026.141599
ER  - 

APA

P, G., AN, L., F, L., C, A., E, B., M, B., L, F., F, Z., & F, B. (2026). Microfluidic confinement enables monitoring of oligomeric forms of 1-40 β-amyloid peptide in kinetic study by AFM.. Journal of colloid and interface science. https://doi.org/10.1016/j.jcis.2026.141599

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