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Structurally Homogeneous Nanosheets from Self‐Assembly of a Collagen‐Mimetic Peptide
Author(s) -
Jiang Tao,
Xu Chunfu,
Zuo Xiaobing,
Conticello Vincent P.
Publication year - 2014
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.201403780
Subject(s) - peptide , nanosheet , homogeneous , aqueous solution , self assembly , domain (mathematical analysis) , sequence (biology) , stereochemistry , population , peptide sequence , chemistry , peptide conformation , materials science , crystallography , nanotechnology , physics , mathematics , organic chemistry , biochemistry , thermodynamics , mathematical analysis , demography , sociology , gene
A collagen‐mimetic peptide, NSIII, has been designed with three sequential blocks having positive, neutral, and negative charges, respectively. The non‐canonical imino acid, (2 S ,4 S )‐4‐aminoproline (amp), was used to specify the positive charges at the Xaa positions of (Xaa‐Yaa‐Gly) triads in the N‐terminal domain of NSIII. Peptide NSIII underwent self‐assembly from aqueous solution to form a highly homogeneous population of nanosheets. Two‐dimensional crystalline sheets formed in which the length of the peptide defined the height of the sheets. These results contrasted with prior results on a similar multi‐domain collagen‐mimetic polypeptides in which the sheets had highly polydisperse distribution of sizes in the ( x / y )‐ and ( z )‐dimensions. The structural differences between the two nanosheet assemblies were interpreted in terms of the relative stereoelectronic effects of the different aminoproline derivatives on the local triple helical conformation of the peptides.