In this section
@article{Mitchell:2026:10.1107/s2053230x26001937,
author = {Mitchell, HM and Nocek, B and Guinn, EJ and Heng, JYY},
doi = {10.1107/s2053230x26001937},
journal = {Acta Crystallographica Section F:Structural Biology Communications},
pages = {114--124},
title = {Crystallization and 1.6Å resolution crystal structure of an acylated GLP-1/GIP analogue peptide},
url = {http://dx.doi.org/10.1107/s2053230x26001937},
volume = {82},
year = {2026}
}
TY - JOUR
AB - With the meteoric rise in interest in GLP-1 and GIP analogue peptides in recent years, there is a drive for the use of alternative purification techniques to alleviate processing bottlenecks and reduce the cost of peptide manufacturing. However, a lack of reported crystal structures for this class of peptides has hindered molecular-scale understanding of GLP-1/GIP analogue peptide crystallization, particularly related to acylated peptides. This paper therefore reports what is believed to be the first crystal structure of a GLP-1 and GIP analogue lipopeptide. Crystals obtained using a microseed matrix-screening protocol diffracted to ≤1.6Å resolution in space group P43, with unit-cell parameters a = b = 64.66, c = 11.42Å. Model building and the resultant structural analysis reveals that the predominantly helical peptide forms a uniquely porous spiral crystal structure composed of clockwise-ascending monomers in a square pattern, with aromatic CH—π interactions around Phe22 forming the primary crystal contact between neighbouring square motifs.
AU - Mitchell,HM
AU - Nocek,B
AU - Guinn,EJ
AU - Heng,JYY
DO - 10.1107/s2053230x26001937
EP - 124
PY - 2026///
SN - 2053-230X
SP - 114
TI - Crystallization and 1.6Å resolution crystal structure of an acylated GLP-1/GIP analogue peptide
T2 - Acta Crystallographica Section F:Structural Biology Communications
UR - http://dx.doi.org/10.1107/s2053230x26001937
UR - https://doi.org/10.1107/s2053230x26001937
VL - 82
ER -