TY - JOUR
T1 - Self-assembly of a cyclo-pentapeptide with a novel frame structure
AU - Yang, Fadeng
AU - Zhang, Pengli
AU - Liu, Jianbo
AU - Wan, Chuan
AU - Sun, Jinming
AU - Dai, Chuan
AU - Liu, Zhihong
AU - An, Yuhao
AU - Wu, Yujie
AU - Xing, Yun
AU - Yin, Feng
AU - Ye, Yuxin
AU - Han, Wei
AU - Li, Zigang
N1 - This work was supported by the National Basic Research Program of China 973 Program (Nos. 2021YFA0910803, 2021YFC2103900), the National Natural Science Foundation of China (No. 21977011), the Natural Science Foundation of Guangdong Province (Nos. 2022A1515010996 and 2020A1515011544), the Shenzhen Science and Technology Innovation Committee (Nos. RCJC20200714114433053, JCYJ20180507181527112 and JCYJ20200109140406047), the Shenzhen-Hong Kong Institute of Brain Science-Shenzhen Fundamental Research Institutions (No. 2019SHIBS0004), the Shenzhen Fundamental Research Program (No. GXWD20201231165807007-20200827170132001), Tian Fu Jin Cheng Laboratory (Advanced Medical Center) Group Racing Project (No. TFJC2023010008).
PY - 2025/9
Y1 - 2025/9
N2 - Developing novel building blocks with predictable side-chain orientations and minimal intramolecular interactions is essential for peptide-based self-assembling materials. Traditional structures like α-helices and β-sheets rely on such interactions for stability, limiting control over exposed interacting moieties. Here, we reported a novel, frame-like peptide scaffold that maintains exceptional stability without intramolecular interactions. This structure exposes its backbone and orients side chains for hierarchical self-assembly into micron-scale cubes. By introducing mutations at specific sites, we controlled packing orientations, offering new options for tunable self-assembly. Our scaffold provides a versatile platform for designing advanced peptide materials, with applications in nanotechnology and biomaterials.
AB - Developing novel building blocks with predictable side-chain orientations and minimal intramolecular interactions is essential for peptide-based self-assembling materials. Traditional structures like α-helices and β-sheets rely on such interactions for stability, limiting control over exposed interacting moieties. Here, we reported a novel, frame-like peptide scaffold that maintains exceptional stability without intramolecular interactions. This structure exposes its backbone and orients side chains for hierarchical self-assembly into micron-scale cubes. By introducing mutations at specific sites, we controlled packing orientations, offering new options for tunable self-assembly. Our scaffold provides a versatile platform for designing advanced peptide materials, with applications in nanotechnology and biomaterials.
KW - Chiral center induced conformation
KW - Cyclo-pentapeptide
KW - Hierarchical packing
KW - Peptide based self-assembly
KW - Rigid frame-like structure
UR - https://www.scopus.com/pages/publications/105008434154
U2 - 10.1016/j.cclet.2024.110785
DO - 10.1016/j.cclet.2024.110785
M3 - Journal article
SN - 1001-8417
VL - 36
JO - Chinese Chemical Letters
JF - Chinese Chemical Letters
IS - 9
M1 - 110785
ER -