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Industrial insulin production uses genetically engineered E. coli expressing a proinsulin gene controlled by a tryptophan promoter and containing a methionine linker for later cleavage. The cells also carry ampicillin resistance for selective growth. Seed cultures are stored at −80 °C and production begins by thawing a small amount to inoculate starter cultures, which are progressively scaled to a 50,000-L bioreactor. In the bioreactor, E. coli grow in nutrient-rich media under sterile, tightly...

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Related Experiment Video

Updated: Jun 13, 2026

Identification of Plant Ice-binding Proteins Through Assessment of Ice-recrystallization Inhibition and Isolation Using Ice-affinity Purification

Identification of Plant Ice-binding Proteins Through Assessment of Ice-recrystallization Inhibition and Isolation Using Ice-affinity Purification

Published on: May 5, 2017

Bioinspired (Glyco)Polypeptides for Ice-Control and Cell Cryopreservation.

Liang Yuan¹, Xiaowen Zhang¹, Lixia Ren¹

¹School of Materials Science and Engineering, Tianjin Key Laboratory of Composite and Functional Materials, Tianjin University, Tianjin, China.

Advanced Materials (Deerfield Beach, Fla.)

|June 12, 2026

Summary

This summary is machine-generated.

Protein-mimetic polypeptides offer advanced cryoprotection for cells, inspired by natural antifreeze proteins. These novel biomaterials enhance cell viability and function after cryopreservation, overcoming limitations of current methods.

Keywords:

cell cryopreservation glycopolypeptides ice‐control macromolecular cryoprotectants polypeptides

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Last Updated: Jun 13, 2026

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Determining the Ice-binding Planes of Antifreeze Proteins by Fluorescence-based Ice Plane Affinity

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Published on: January 15, 2014

Area of Science:

Biomaterials Science
Cryobiology
Polymer Chemistry

Background:

Cryopreservation is vital for biomedical research and clinical applications.
Current cryoprotective agents face challenges in efficiency and biocompatibility for diverse cell types.
Antifreeze proteins inspire new strategies for cellular cryopreservation.

Purpose of the Study:

To review the synthesis, structure, and self-assembly of (glyco)polypeptides as macromolecular cryoprotectants.
To highlight the ice-controlling properties and cryoprotective mechanisms of these biomaterials.
To discuss the prospects of multifunctional (glyco)polypeptides in cell cryopreservation.

Main Methods:

Review of literature on (glyco)polypeptide synthesis and characterization.
Analysis of studies on ice nucleation, shaping, and recrystallization inhibition by (glyco)polypeptides.
Evaluation of cryopreservation performance data for various cell types using these agents.

Main Results:

(Glyco)polypeptides exhibit protein-mimetic structures, offering biocompatibility and tunable properties.
These polymers effectively control ice formation processes, including nucleation, shaping, and recrystallization inhibition.
Demonstrated efficacy in maintaining cellular viability and function post-cryopreservation.

Conclusions:

(Glyco)polypeptides represent a promising class of macromolecular cryoprotectants with significant advantages over traditional methods.
Further research into structure-property relationships and machine learning integration can optimize their application.
These biomaterials hold potential for advancing cell storage in both research and clinical settings.