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The effects of alpha-helix on the stability of Asn residues: Deamidation rates in peptides of varying helicity

Published online by Cambridge University Press:  01 November 1999

ANDREW A. KOSKY ,
URSULA O. RAZZAQ ,
MICHAEL J. TREUHEIT  and
DAVID N. BREMS
ANDREW A. KOSKY
Affiliation:
Amgen Inc., Thousand Oaks, California 91320
URSULA O. RAZZAQ
Affiliation:
Amgen Inc., Thousand Oaks, California 91320
MICHAEL J. TREUHEIT
Affiliation:
Amgen Inc., Thousand Oaks, California 91320
DAVID N. BREMS
Affiliation:
Amgen Inc., Thousand Oaks, California 91320
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Abstract

Asn deamidation was monitored in Ala-based octadecapeptides of varying α-helicity. Gly was substituted for Ala residues at positions 6 and 16 to create a peptide with less helicity. Ala → Gly substitutions were made at three or more residues from the Asn to negate known primary sequence effects on deamidation rates. The extent of helicity and rate of Asn deamidation for alkaline aqueous solutions of each peptide was measured as a function of temperature by circular dichroism and reversed-phase high-performance liquid chromatography, respectively. The rate of deamidation in the peptides was inversely proportional to the extent of α-helicity. The results support the conclusion that Asn deamidation only occurs in the nonhelical population of conformers.

Keywords

α-helicitydeamidationpeptidessuccinimide
Type
Research Article
Information
Protein Science , Volume 8 , Issue 11 , November 1999 , pp. 2519 - 2523
Copyright
© 1999 The Protein Society

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