Validation of molecular force field parameters for peptides including isomerized amino acids

Author:

Oda Akifumi123ORCID,Nakayoshi Tomoki12,Fukuyoshi Shuichi2,Kurimoto Eiji1,Yamaotsu Noriyuki4ORCID,Hirono Shuichi4,Takahashi Ohgi5

Affiliation:

1. Faculty of Pharmacy; Meijo University; Nagoya Aichi Japan

2. Institute of Medical, Pharmaceutical and Health Sciences; Kanazawa University; Kanazawa Ishikawa Japan

3. Institute for Protein Research; Osaka University; Osaka Japan

4. School of Pharmacy; Kitasato University; Tokyo Japan

5. Faculty of Pharmaceutical Sciences; Tohoku Medical and Pharmaceutical University; Sendai Miyagi Japan

Funder

Japan Society for the Promotion of Science

Publisher

Wiley

Subject

Organic Chemistry,Spectroscopy,Drug Discovery,Pharmacology,Catalysis,Analytical Chemistry

Reference27 articles.

1. Homochirality and life;Fujii;Chem Rec,2004

2. Structural alterations in the peptide backbone of β-amyloid core protein may account for its deposition and stability in Alzheimer's disease;Roher;J Biol Chem,1993

3. Racemization of Asp23 residue affects the aggregation properties of Alzheimer amyloid β protein analogues;Tomiyama;J Biol Chem,1994

4. Racemization of the amyloidal β Asp1 residue blocks the acceleration of fibril formation caused by racemization of the Asp23 residue;Sakai-Kato;Biochem Biophys Res Commun,2007

5. Simultaneous stereoinversion and isomerization at specific aspartic acid residues in αA-crystallin from human lens;Fujii;J Biochem,1994

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