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A Short C-Terminal Region of Alpha-Synuclein Protects a (R/S)-Nonspecific Esterase from Archaeglobus fulgidus

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We show that α-synuclein could assist the molecular activity of a ketoprofen-(R/S) nonspecific esterase from Archaeglobus Fulgidus. Specifically, several synthetic peptides from α-synuclein, each having random coil conformation in far-UV spectra, could protect the enzyme activity against stress conditions such as heat and organic solvents.

Keywords: esterase; molecular engineering; protective activity; α-Synuclein

Document Type: Research Article

DOI: http://dx.doi.org/10.2174/092986607780363880

Affiliations: Division of Biotechnology and Molecular Engineering, College of Engineering, Ajou University, Suwon,South Korea.

Publication date: April 1, 2007

More about this publication?
  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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