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Gel‐ and Solid‐State‐Structure of Dialanine and Diphenylalanine Amphiphiles: Importance of C⋅⋅⋅H Interactions in Gelation
Author(s) -
Farahani Abbas D.,
Martin Adam D.,
Iranmanesh Hasti,
Bhadbhade Mohan M.,
Beves Jonathon E.,
Thordarson Pall
Publication year - 2019
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.201801104
Subject(s) - peptide , circular dichroism , chemistry , crystallography , self assembly , amphiphile , methylene , self healing hydrogels , solid state , naphthalene , stereochemistry , organic chemistry , polymer , copolymer , biochemistry
To investigate the role of the capping group in the solution and solid‐state self‐assembly of short peptide amphiphiles, dialanine and diphenylalanine have been linked via the N‐terminus to a benzene (phenyl) and 3‐naphthyl capping groups using three different methylene linkers; (CH 2 ) n , n =0–4 for the benezene and 0, 1 and 2 for the naphthalene capping group. Atomic force microscopy (AFM), oscillatory rheology, circular dichroism (CD), and IR analysis have been employed to understand the properties of these peptide‐based hydrogels. Several X‐ray structures of these short peptide gelators give useful conformational information regarding packing. A comparison of these solid state structures with their gel state properties yielded greater insights into the process of self‐assembly in short peptide gelators, particularly in terms of the important role of C⋅⋅⋅H interactions appear to play in determining if a short aromatic peptide does form a gel or not.