The extinction coefficient of N-methylated Aβ30-40 depends on the position of N-methylation

Hironori Ochiai; Tomoyuki Komuro; Hirotsugu Hiramatsu

doi:10.1246/cl.140851

The extinction coefficient of N-methylated Aβ_30-40 depends on the position of N-methylation

Hironori Ochiai, Tomoyuki Komuro, Hirotsugu Hiramatsu

PHA - Molecular Pharmaceutical Science

Research output: Contribution to journal › Article › peer-review

1 Citation (Scopus)

Abstract

The molar extinction coefficient at 210 nm (σ₂₁₀) of the N-methylated analogs of Aβ_30-40 was analyzed. Additive contributions from a 10-residue peptide main chain (σ₂₁₀ ^CONH) and modulation caused by N-methylation (Δσ₂₁₀) accounted for the observed results. The observed σ₂₁₀ ^CONH value was concordant with reported values. The difference in the Δσ₂₁₀ value was explained in terms of changes in electronic structure and conformational restriction resulting from N-methylation.

Original language	English
Pages (from-to)	35-37
Number of pages	3
Journal	Chemistry Letters
Volume	44
Issue number	1
DOIs	https://doi.org/10.1246/cl.140851
Publication status	Published - 2015

ASJC Scopus subject areas

Chemistry(all)

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title = "The extinction coefficient of N-methylated Aβ30-40 depends on the position of N-methylation",

abstract = "The molar extinction coefficient at 210 nm (σ210) of the N-methylated analogs of Aβ30-40 was analyzed. Additive contributions from a 10-residue peptide main chain (σ210 CONH) and modulation caused by N-methylation (Δσ210) accounted for the observed results. The observed σ210 CONH value was concordant with reported values. The difference in the Δσ210 value was explained in terms of changes in electronic structure and conformational restriction resulting from N-methylation.",

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AB - The molar extinction coefficient at 210 nm (σ210) of the N-methylated analogs of Aβ30-40 was analyzed. Additive contributions from a 10-residue peptide main chain (σ210 CONH) and modulation caused by N-methylation (Δσ210) accounted for the observed results. The observed σ210 CONH value was concordant with reported values. The difference in the Δσ210 value was explained in terms of changes in electronic structure and conformational restriction resulting from N-methylation.

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