Imperial College London
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Professor Jerry Heng

Faculty of Engineering, Department of Chemical Engineering

Professor in Particle Technology
 
 
 
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Contact

 

+44 (0)20 7594 0784jerry.heng

 
 
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Location

 

208ACE ExtensionSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Guo:2023:10.1021/acs.cgd.2c01229,
author = {Guo, M and Jones, MJ and Goh, R and Verma, V and Guinn, E and Heng, JYY},
doi = {10.1021/acs.cgd.2c01229},
journal = {Crystal Growth and Design},
pages = {1668--1675},
title = {The effect of chain length and conformation on the nucleation of glycine homopeptides during the crystallization process.},
url = {http://dx.doi.org/10.1021/acs.cgd.2c01229},
volume = {23},
year = {2023}
}
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RIS format (EndNote, RefMan)

TY  - JOUR
AB  - To explore the effect of chain length and conformation on the nucleation of peptides, the primary nucleation induction time of glycine homopeptides in pure water at different supersaturation levels under various temperatures has been determined. Nucleation data suggest that longer chains will prolong the induction time, especially for chains longer than three, where nucleation will occur over several days. In contrast, the nucleation rate increased with an increase in the supersaturation for all homopeptides. Induction time and nucleation difficulty increase at lower temperatures. However, for triglycine, the dihydrate form was produced with an unfolded peptide conformation (pPII) at low temperature. The interfacial energy and activation Gibbs energy of this dihydrate form are both lower than those at high temperature, while the induction time is longer, indicating the classical nucleation theory is not suitable to explain the nucleation phenomenon of triglycine dihydrate. Moreover, gelation and liquid-liquid separation of longer chain glycine homopeptides were observed, which was normally classified to nonclassical nucleation theory. This work provides insight into how the nucleation process evolves with increasing chain length and variable conformation, thereby offering a fundamental understanding of the critical peptide chain length for the classical nucleation theory and complex nucleation process for peptides.
AU  - Guo,M
AU  - Jones,MJ
AU  - Goh,R
AU  - Verma,V
AU  - Guinn,E
AU  - Heng,JYY
DO  - 10.1021/acs.cgd.2c01229
EP  - 1675
PY  - 2023///
SN  - 1528-7483
SP  - 1668
TI  - The effect of chain length and conformation on the nucleation of glycine homopeptides during the crystallization process.
T2  - Crystal Growth and Design
UR  - http://dx.doi.org/10.1021/acs.cgd.2c01229
UR  - https://www.ncbi.nlm.nih.gov/pubmed/36879769
UR  - https://pubs.acs.org/doi/10.1021/acs.cgd.2c01229
UR  - http://hdl.handle.net/10044/1/103641
VL  - 23
ER  -
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