# Preparation of Self-Assembled Human Serum Albumin Nanoparticles Decorated with Trastuzumab as a Paclitaxel Delivery System

## TL;DR

Researchers created HSA nanoparticles decorated with trastuzumab to deliver paclitaxel, showing high drug efficiency and potential for targeted cancer therapy.

## Contribution

A novel HSA nanoparticle system decorated with trastuzumab for targeted paclitaxel delivery was developed and characterized.

## Key findings

- HSA-PTX and HSA-PTX-TMAB nanoparticles showed high drug association efficiency (96.4% and 98.2%, respectively).
- TMAB decoration increased mean diameter and reduced surface charge, confirming successful surface modification.
- Both formulations exhibited rapid initial PTX release followed by a stabilization phase with distinct kinetic behavior.

## Abstract

This study reports the development of paclitaxel (PTX)-loaded human serum albumin (HSA) nanoparticles (NPs), surface-decorated with trastuzumab (TMAB), with potential applicability in HER2-oriented delivery. The NPs were obtained via thermally driven self-assembly followed by non-covalent antibody adsorption and they were characterized using Fourier transform infrared spectroscopy (FTIR), dynamic light scattering (DLS), and ζ-potential analysis. The drug association efficiency (%DAE), defined exclusively for PTX, was high for both HSA-PTX and HSA-PTX-TMAB NPs (96.4% and 98.2% w/w, respectively), with loading capacities (%LC) of 8.9% and 7.4%, respectively. TMAB decoration led to a modest increase in mean diameter and a reduction in surface charge, consistent with successful surface modification. Both formulations exhibited rapid early-phase PTX release followed by an apparent stabilization phase, with distinct kinetic behavior between HSA–PTX and HSA–PTX–TMAB NPs. Cytotoxicity in A549 cells after 18 h of exposure showed modest, non-differential effects consistent with controlled release and short-term assessment of non-specific toxicity. Overall, this thermally assembled albumin-based system provides a promising foundation for further evaluation of HER2-oriented PTX delivery.