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Protein and Protein Structure

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Proteins are one of the most abundant organic molecules in living systems and have the most diverse range of functions of all macromolecules. Proteins may be structural, regulatory, contractile, or protective. They may serve in transport, storage, or membranes; or they may be toxins or enzymes. Their structures, like their functions, vary greatly. They are all, however, amino acid polymers arranged in a linear sequence.
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Injectable Supramolecular Polymer-Nanoparticle Hydrogels for Cell and Drug Delivery Applications

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The relation between moisture-induced aggregation and structural changes in lyophilized insulin.

Giselle M Flores-Fernández¹, Ricardo J Solá, Kai Griebenow

¹Department of Chemistry, University of Puerto Rico, Río Piedras Campus, San Juan, Puerto Rico.

The Journal of Pharmacy and Pharmacology

|November 12, 2009

Summary

Moisture exposure causes structural changes in lyophilized insulin, leading to protein aggregation and inactivation. Understanding these solid-state instability effects is crucial for pharmaceutical development.

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Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders

Mass Spectrometric Approaches to Study Protein Structure and Interactions in Lyophilized Powders

Published on: April 14, 2015

Area of Science:

Pharmaceutical Science
Protein Chemistry
Analytical Chemistry

Background:

Protein pharmaceuticals require long-term stability, often achieved through lyophilization.
Lyophilized protein powders are susceptible to moisture, causing aggregation and loss of activity.
Investigating the impact of moisture on solid-state protein structure is vital for formulation development.

Purpose of the Study:

To investigate the structural consequences of moisture sorption in lyophilized insulin.
To correlate structural changes with solid-state instability under controlled humidity.
To understand the role of water in protein aggregation during storage.

Main Methods:

Lyophilized insulin samples were exposed to controlled humidity at 50°C.
Fourier transform-infrared (FT-IR) microscopy analyzed secondary structural changes.
Near-UV circular dichroism assessed tertiary structure.
Protein aggregation was quantified by measuring soluble and insoluble fractions.

Main Results:

Low humidity (11%) induced minor structural changes in lyophilized insulin.
Higher humidity levels caused significant alterations, including loss of alpha-helix and gain of beta-sheet content.
Observed structural changes correlated with increased protein aggregation and loss of tertiary structure upon reconstitution.

Conclusions:

Water sorption facilitates structural transitions in lyophilized proteins.
These transitions are linked to protein aggregation and inactivation.
Controlling moisture is critical for maintaining the stability of lyophilized protein pharmaceuticals.