Recovery and purification of highly aggregation-prone disulfide-containing peptides: Application to islet amyloid polypeptide

Author:

Abedini Andisheh,Singh Gagandeep,Raleigh Daniel P.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry,Biophysics

Reference33 articles.

1. Cyclization of disulfide-containing peptides in solid-phase synthesis;Albericio;Int. J. Pept. Protein Res.,1991

2. Semchuk, P.D., Monera, O.D., Kondejewski, L.H., Daniels, L., Wilson, I., Hodges, R.S., 1995. Peptides: Chemistry, Structure and Biology, Proceedings of the American Peptide Symposium, 14th, Columbus, Ohio.

3. Dimethyl(methylthio)sulfonium tetrafluoroborate: a reagent for disulfide bond formation in peptides;Bishop;Tetrahedron Lett.,1993

4. Seeding specificity in amyloid growth induced by heterologous fibrils;O’Nuallain;J. Biol. Chem.,2004

5. Incorporation of pseudoproline derivatives allows the facile synthesis of human IAPP, a highly amyloidogenic and aggregation-prone polypeptide;Abedini;Org. Lett.,2005

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