Self-assembly of aromatic amino acids: a molecular dynamics study
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Tarih
2018
Dergi Başlığı
Dergi ISSN
Cilt Başlığı
Yayıncı
Royal Soc Chemistry
Erişim Hakkı
info:eu-repo/semantics/closedAccess
Özet
The self assembly processes of aromatic amino acids, phenylalanine, tyrosine, and tryptophan have been simulated and were observed to form fibril-like aggregates linked to certain rare diseases and instances of biological membrane disruption. Pure systems and their mixtures were studied systematically at constant temperatures and free energy landscapes were produced describing the height and the number of assembled monomers associated with lower energy structures. Consistent with some previous work, aromatic amino acid monomers display a tendency to arrange with a four-fold symmetry. The occurrence of this and other ordered structures increases at higher temperatures. At lower temperatures our binary mixture simulations indicate that increasing tryptophan content drives the assembly process away from the formation of distinct nanostructures and toward disordered aggregates which is in line with experimental observations of pure tryptophan solutions. This work provides molecular level insight to a variety of different physical phenomena relevant to fields including human disease.
Açıklama
Hernandez, Helen/0000-0001-5751-3470
WOS:000453231100042
PubMed: 30512023
WOS:000453231100042
PubMed: 30512023
Anahtar Kelimeler
Kaynak
Physical Chemistry Chemical Physics
WoS Q Değeri
Q1
Scopus Q Değeri
Q1
Cilt
20
Sayı
48
