The plot thickens: Gelation by phenylalanine in water and dimethyl sulfoxide

Nartowski, Karol P., Ramalhete, Susana M., Martin, Peter C., Foster, Jamie S., Heinrich, Margaux, Eddleston, Mark D., Green, Hayley R., Day, Graeme M., Khimyak, Yaroslav Z. ORCID: https://orcid.org/0000-0003-0424-4128 and Lloyd, Gareth O. (2017) The plot thickens: Gelation by phenylalanine in water and dimethyl sulfoxide. Crystal Growth & Design, 17 (8). 4100–4109. ISSN 1528-7483

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Abstract

Phenylalanine (Phe) is an amino acid of great interest as coupling of an aromatic group with a chiral hydrophilic region imparts a number of unique properties. Recently there has been an increased interest in the crystalline and gel forms of this compound, part as a result of the complex and undetermined structures of the resulting materials and the relationship of the solid forms of Phe with the disease phenylketonuria. In this report, we highlight the relationship between gelation, crystallization, and the dynamics of self-assembly processes of Phe. We do this by describing the gelation of the amino acid, the gel to crystal relationship, crystal structure predictions for this relatively simple compound, and the dynamics of assembly as determined by NMR in both water and dimethyl sulfoxide. This will provide guidance to future research into Phe assemblies, possible treatments for phenylketonuria, and diseases related to formation of amyloid-like fibers.

Item Type:	Article
Uncontrolled Keywords:	phenylalanine,gel,lmwg,self-assembly,crystallisation,crystal structure prediction,csp,nmr crystallography
Faculty \ School:	Faculty of Science > School of Pharmacy (former - to 2024)
UEA Research Groups:	Faculty of Science > Research Groups > Drug Delivery and Pharmaceutical Materials (former - to 2017) Faculty of Science > Research Groups > Pharmaceutical Materials and Soft Matter
Depositing User:	Pure Connector
Date Deposited:	25 Jul 2017 05:09
Last Modified:	25 Oct 2024 23:45
URI:	https://ueaeprints.uea.ac.uk/id/eprint/64237
DOI:	10.1021/acs.cgd.7b00213

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