Interactions of human serum albumin with phosphate and Tris buffers: impact on paclitaxel binding and nanoparticles self-assembly

Buffer type and pH significantly influence NP properties. TD in PBS at pH 7.4, provided optimal conditions for a stable and efficient drug delivery system.

Authors

Mónica Mesa (ORCID: https://orcid.org/0000-0002-6175-6384)
Ligia Sierra (ORCID: https://orcid.org/0000-0002-0902-9868)
A. H. Gonzalez-Posada

Institutions

Universidad de Antioquia (CO)

Publication Details

Journal: Journal of Microencapsulation
Published: 2024-09-13
DOI: https://doi.org/10.1080/02652048.2024.2389135
Citations: 1
Primary Topic: Protein Interaction Studies and Fluorescence Analysis
Type: article
Field-Weighted Citation Impact: 0.23

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article

Interactions of human serum albumin with phosphate and Tris buffers: impact on paclitaxel binding and nanoparticles self-assembly

Mónica Mesa, Ligia Sierra, A. H. Gonzalez-Posada

Sep 13, 2024

1 citations

Journal of Microencapsulation

Protein Interaction Studies and Fluorescence Analysis

0.23

article

Interactions of human serum albumin with phosphate and Tris buffers: impact on paclitaxel binding and nanoparticles self-assembly

Mónica Mesa, Ligia Sierra, A. H. Gonzalez-Posada

September 13, 2024article en

1 citations

Abstract

Buffer type and pH significantly influence NP properties. TD in PBS at pH 7.4, provided optimal conditions for a stable and efficient drug delivery system.

Journal of MicroencapsulationVol. 41(7)

Universidad de Antioquia (CO)

Openalex Percentile: Top 43%

Protein Interaction Studies and Fluorescence Analysis

0.23

DOI Source OpenAlex

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Interactions of human serum albumin with phosphate and Tris buffers: impact on paclitaxel binding and nanoparticles self-assembly — Mónica Mesa, Ligia Sierra, et al. · Journal of Microencapsulation (2024) | TGRS Research Map | TGRS