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Thermodynamic and Structural Impact of ?,?-Dialkylated Residue Incorporation in a ?-Hairpin Peptide.

ABSTRACT: Peptides containing ?,?-dialkylated ?-amino acids, owing to their ability to disrupt aggregation of ?-amyloid proteins, have therapeutic potential in the treatment of neurodegenerative diseases. Thermodynamic and structural analyses are reported for a series of ?-hairpin peptides containing ?,?-dialkylated ?-amino acids with varying side-chain lengths. The results of these experiments show that ?,?-dialkylated ?-amino acids with side-chain lengths longer than one carbon unit are tolerated in a ?-hairpin, although at a moderate cost to folded stability.

SUBMITTER: Karnes MA

PROVIDER: S-EPMC4975614 | biostudies-literature | 2016 Aug

REPOSITORIES: biostudies-literature

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Thermodynamic and Structural Impact of α,α-Dialkylated Residue Incorporation in a β-Hairpin Peptide.

Karnes Megan A MA Schettler Shelby L SL Werner Halina M HM Kurz Alana F AF Horne W Seth WS Lengyel George A GA

Organic letters 20160720 15

Peptides containing α,α-dialkylated α-amino acids, owing to their ability to disrupt aggregation of β-amyloid proteins, have therapeutic potential in the treatment of neurodegenerative diseases. Thermodynamic and structural analyses are reported for a series of β-hairpin peptides containing α,α-dialkylated α-amino acids with varying side-chain lengths. The results of these experiments show that α,α-dialkylated α-amino acids with side-chain lengths longer than one carbon unit are tolerated in a β ...[more]

PMID: 27436716

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