Peer-reviewedCC BY-NC-NDACS omega1 Oct 2026

Design and Characterization of Bovine Serum Albumin Hydrogels: A Promising Platform for Controlled Drug Delivery

Eva M. M. Velez^1,2
María C. Maldonado Galdeano²
Rosana Chehín¹
Silvina Chaves¹

¹Instituto de Investigación en Medicina Molecular y Celular Aplicada (IMMCA) (CONICET), Universidad Nacional de Tucumán (UNT), Ministerio de Salud Pública de Tucumán - SIPROSA , Pasaje Dorrego 1080 , , ,
²Centro de Referencia para Lactobacilos (CERELA-CONICET) , Batalla de Chacabuco 145 , , ,

Abstract

Protein-based hydrogels have attracted increasing interest as biocompatible matrices for drug delivery; however, simple systems based exclusively on albumin remain relatively underexplored. Here, we report the formation of bovine serum albumin (BSA) hydrogels generated through mild thermal aggregation (65 °C) without chemical cross-linkers, employing low protein concentrations (1–1.5%). The influence of the buffering environment (PBS vs Tris-HCl) on hydrogel architecture was identified as a key structural determinant. The resulting hydrogels were systematically characterized in terms of their structure, swelling behavior, water content, biodegradability, and morphology. Microscopic analyses revealed that Tris-HCl promoted the formation of a homogeneous and dense amyloid-like fibrillar network, whereas PBS led to more heterogeneous and irregular architectures. These structural differences affected the capacity to absorb and release model compounds with distinct physicochemical properties, producing sustained and matrix-dependent release profiles. In vitro assays demonstrated progressive degradation under physiological conditions, while in vivo murine models showed minimal immunological response.

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BibTeX RIS

BibTeX

@article{velez2026design,
  title = {{Design and Characterization of Bovine Serum Albumin Hydrogels: A Promising Platform for Controlled Drug Delivery}},
  author = {Eva M. M. Velez and María C. Maldonado Galdeano and Rosana Chehín and Silvina Chaves},
  journal = {ACS omega},
  year = {2026},
  month = oct,
  doi = {10.1021/acsomega.5c11084},
  url = {https://europepmc.org/article/PMC/PMC13670805},
  note = {CC BY-NC-ND},
}

RIS

TY  - JOUR
TI  - Design and Characterization of Bovine Serum Albumin Hydrogels: A Promising Platform for Controlled Drug Delivery
AU  - Eva M. M. Velez
AU  - María C. Maldonado Galdeano
AU  - Rosana Chehín
AU  - Silvina Chaves
PY  - 2026
DA  - 2026/10/01
JO  - ACS omega
DO  - 10.1021/acsomega.5c11084
UR  - https://europepmc.org/article/PMC/PMC13670805
AB  - Protein-based hydrogels have attracted increasing interest as biocompatible matrices for drug delivery; however, simple systems based exclusively on albumin remain relatively underexplored. Here, we report the formation of bovine serum albumin (BSA) hydrogels generated through mild thermal aggregation (65 °C) without chemical cross-linkers, employing low protein concentrations (1–1.5%). The influence of the buffering environment (PBS vs Tris-HCl) on hydrogel architecture was identified as a key structural determinant. The resulting hydrogels were systematically characterized in terms of their structure, swelling behavior, water content, biodegradability, and morphology. Microscopic analyses revealed that Tris-HCl promoted the formation of a homogeneous and dense amyloid-like fibrillar network, whereas PBS led to more heterogeneous and irregular architectures. These structural differences affected the capacity to absorb and release model compounds with distinct physicochemical properties, producing sustained and matrix-dependent release profiles. In vitro assays demonstrated progressive degradation under physiological conditions, while in vivo murine models showed minimal immunological response.
SN  - 2470-1343
ER  -

Abstract

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