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Demonstration of a 1-3 disulfide bond in a synthetic nonapeptide derived from the signal sequence and N-terminus of human gamma-interferon.

Abstract：

:The nonapeptide Cys-Tyr-Cys-Gln-Asp-Pro-Tyr-Val-Lys was prepared by solid-phase peptide synthesis under oxidizing conditions. Fast atom bombardment mass spectrometric analysis of the untreated molecule produced an ion consistent with a structure involving an intramolecular disulfide bond between Cys(1) and Cys(3). Mass spectra of the peptide after treatment with 2-mercaptoethanol gave signals corresponding to the reduced disulfide form of the peptide and to a mixed disulfide of the peptide with 2-mercaptoethanol. Molecular mechanics calculations of the conformation of the 11-membered ring formed by disulfide bond closure predicted a discrete, low-energy structure resembling the locus of a gamma turn. We hypothesize that this structure may be important in the recognition and cleavage of the signal sequence of the parent molecule.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Pramanik B,Tsarbopoulos A,Labdon JE,Czarniecki M,Nagabhushan TL,Trotta PP

doi

10.1016/s0006-291x(88)80325-5

subject

Has Abstract

pub_date

1988-12-15 00:00:00

pages

836-43

issue

2

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(88)80325-5

journal_volume

157

pub_type

杂志文章

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