TY - JOUR
T1 - A Perspective on Interdicting in Protein Misfolding for Therapeutic Drug Design
T2 - Modulating the Formation of Nonlocal Contacts in α-Synuclein as a Strategy against Parkinson’s Disease
AU - Bergasa-Caceres, Fernando
AU - Rabitz, Herschel A.
N1 - Publisher Copyright:
© 2024 American Chemical Society.
PY - 2024/7/11
Y1 - 2024/7/11
N2 - In recent work we proposed that interdiction in the earliest contact-formation events along the folding pathway of key viral proteins could provide a novel avenue for therapeutic drug design. In this Perspective we explore the potential applicability of the protein folding interdiction strategy in the realm of neurodegenerative diseases with a specific focus on synucleinopathies. In order to fulfill this goal we review the interdiction proposal and its practical challenges, and we present new results concerning design strategies for possible peptide drugs that could be useful in preventing α-synuclein aggregation.
AB - In recent work we proposed that interdiction in the earliest contact-formation events along the folding pathway of key viral proteins could provide a novel avenue for therapeutic drug design. In this Perspective we explore the potential applicability of the protein folding interdiction strategy in the realm of neurodegenerative diseases with a specific focus on synucleinopathies. In order to fulfill this goal we review the interdiction proposal and its practical challenges, and we present new results concerning design strategies for possible peptide drugs that could be useful in preventing α-synuclein aggregation.
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U2 - 10.1021/acs.jpcb.3c07519
DO - 10.1021/acs.jpcb.3c07519
M3 - Review article
C2 - 38940731
AN - SCOPUS:85197074999
SN - 1520-6106
VL - 128
SP - 6439
EP - 6448
JO - Journal of Physical Chemistry B
JF - Journal of Physical Chemistry B
IS - 27
ER -