The structural characteristics of nonspecific lipid transfer proteins explain their resistance to gastroduodenal proteolysis.

Biochemistry
Ramani Wijesinha-BettoniE N Clare Mills

Abstract

The structure and stability of the allergenic nonspecific lipid transfer protein (LTP) of peach were compared with the homologous LTP1 of barley and its liganded form LTP1b. All three proteins were resistant to gastric pepsinolysis and were only slowly digested at 1 to 2 out of 14 potential tryptic and chymotryptic cleavage sites under duodenal conditions. Peach LTP was initially cleaved at Tyr79-Lys80 and then at Arg39-Thr40 (a site lost in barley LTP1). Molecular dynamics simulations of the proteins under folded conditions showed that the backbone flexibility is limited, explaining the resistance to duodenal proteolysis. Arg39 and Lys80 side chains were more flexible in simulations of peach compared with barley LTP1. This may explain differences in the rates of cleavage observed experimentally for the two proteins and suggests that the flexibility of individual amino acid side chains could be important in determining preferred proteolytic cleavage sites. In order to understand resistance to pepsinolysis, proteins were characterized by NMR spectroscopy at pH 1.8. This showed that the helical regions of both proteins remain folded at this pH. NMR hydrogen exchange studies confirmed the rigidity of the structures at acidic pH, w...Continue Reading

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Citations

Apr 4, 2013·International Archives of Allergy and Immunology·D G EboL S De Clerck
Jul 7, 2012·PloS One·Stefano AlessandriKarin Hoffmann-Sommergruber
Nov 28, 2012·Clinical Reviews in Allergy & Immunology·R Christopher Van Winkle, Christopher Chang
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Jun 8, 2017·International Journal of Molecular Sciences·Sarina GrutschMartin Tollinger
Sep 4, 2016·Allergy·I I DecuyperD G Ebo

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