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Insulin aggregation in solution.

M Dathe¹, K Gast, D Zirwer

¹Institute of Drug Research, Academy of Sciences of the GDR, Berlin.

International Journal of Peptide and Protein Research

|October 1, 1990

Summary

Insulin aggregation in neutral solutions was studied. Unexpectedly, distinct 100 nm insulin particles formed after a lag phase, suggesting a transient state in solution destabilization.

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Area of Science:

Biochemistry
Physical Chemistry
Materials Science

Background:

Insulin aggregation is a critical concern for therapeutic protein stability.
Understanding the physical processes of insulin aggregation is essential for drug formulation.

Purpose of the Study:

To investigate the aggregation process of insulin in neutral solutions under stress.
To characterize the size and formation kinetics of insulin aggregates.

Main Methods:

Dynamic light scattering (DLS) was employed to monitor particle size distributions.
Insulin solutions were subjected to thermal (37°C) and mechanical (rotation) stress for 4 weeks.
Scattering intensity and particle size were analyzed over time.

Main Results:

Initial insulin solutions contained hexamers; aggregation initiated after an ~8-day lag period.
Scattering intensity increased, but no perceptible turbidity developed.
Distinct 100 nm-sized insulin particles emerged, increasing over time, particularly in diluted solutions.
Aggregate formation correlated with adsorption to solid interfaces.

Conclusions:

Insulin aggregation in neutral solutions is not a continuous growth process.
The formation of 100 nm particles appears to be a transient intermediate state.
Adsorption phenomena play a role in the physical destabilization of insulin solutions.

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