Aging-Dependent Morphological Crystallinity Determines Membrane Activity of l‑Phenylalanine Self-Assembles

Amyloid polymorphism has emerged as an important topic of research in recent years to identify the particular species responsible for several neurodegenerative disorders, whereas the concept is overlooked in the case of the simplest building block, that is, l-phenylalanine (l-Phe) self-assembly. Her...

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Bibliographic Details
Published in:The journal of physical chemistry letters 2020-10, Vol.11 (20), p.8585-8591
Main Authors: Banerjee, Pavel, Rajak, Karunamoy, Nandi, Pratyush Kiran, Pal, Siddhartha, Ghosh, Meghna, Mishra, Sabyashachi, Sarkar, Nilmoni
Format: Article
Language:English
Subjects:
Age Factors
Amyloid - chemistry
Crystallization
Humans
Hydrogen Bonding
Optical Imaging
Phenylalanine - chemistry
Phenylketonurias - metabolism
Physical Insights into Materials and Molecular Properties
Protein Binding
Protein Conformation
Protein Folding
Protein Multimerization
Temperature
Thermodynamics
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Summary:Amyloid polymorphism has emerged as an important topic of research in recent years to identify the particular species responsible for several neurodegenerative disorders, whereas the concept is overlooked in the case of the simplest building block, that is, l-phenylalanine (l-Phe) self-assembly. Here, we report the first evidence of l-Phe polymorphism and the conversion of metastable helical fibrillar to thermodynamically stable rodlike crystalline morphologies with increasing time and temperature. Furthermore, only the fibrillar l-Phe polymorph shows a significant modulation of the model membrane. In addition, the l-Phe molecules prefer to arrange in a multilayered rodlike fashion than in a lateral arrangement, which reduces the membrane binding ability of the l-Phe polymorph due to the decrease in the partial charge of the N-terminal of l-Phe units. The present work exemplifies a different approach to understanding l-Phe self-assembly and provides an effective strategy for the therapy of phenylketonuria by scrutinizing the discrete membrane activity of different l-Phe polymorphs.
ISSN:1948-7185
1948-7185
DOI:10.1021/acs.jpclett.0c01831