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Thermo-Optical Protein Characterization for Straightforward Preformulation Development.

Randy Wanner¹, Dennis Breitsprecher², Stefan Duhr²

¹Ludwig-Maximilians-Universität München, Department of Pharmacy, Pharmaceutical Technology and Biopharmaceutics, Butenandtstrasse 5, Munich 81377, Germany.

Journal of Pharmaceutical Sciences

|June 19, 2017

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A novel thermo-optical method efficiently assesses protein unfolding and aggregation during biopharmaceutical preformulation. This label-free technique saves time and material, aiding early drugability screenings.

Area of Science:

Biopharmaceutical Development
Protein Science
Analytical Chemistry

Background:

Protein unfolding and aggregation are critical factors in biopharmaceutical formulation.
Early-stage screening methods are needed for efficient drug development.

Purpose of the Study:

To evaluate a new immobilization- and label-free thermo-optical approach.
To assess its utility for material- and time-saving early formulation and drugability screenings.

Main Methods:

Utilized intrinsic tryptophan fluorescence changes during IR laser-induced heating.
Measured protein unfolding, aggregation, and precipitation signals over time.
Compared results with forced degradation and thermal stability data.

Keywords:

biopharmaceuticals characterization fluorescence spectroscopy high-throughput technologies monoclonal antibody pH physical stability preformulation protein aggregation protein folding/refolding protein formulation

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Main Results:

Thermo-optical signals correlated well with aggregation propensity and unfolding reversibility.
The method demonstrated separable effects of unfolding, aggregation, and precipitation.
Successful analysis with minimal sample volume (4 μL) and short measurement time (150 s).

Conclusions:

The thermo-optical approach is a feasible orthogonal method for biopharmaceutical preformulation.
It offers potential for rapid candidate and formulation selection.
The technique is applicable for early-stage drugability assessments.